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Molecular Fluorescence, Phosphorescence, and
Chemiluminescence Spectrometry
Article in Analytical Chemistry · July 2008
DOI: 10.1021/ac800749v · Source: PubMed
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Anal. Chem. 2008, 80, 4551–4574
Molecular Fluorescence, Phosphorescence, and
Chemiluminescence Spectrometry
Mark Lowry,† Sayo O. Fakayode,‡ Maxwell L. Geng,§ Gary A. Baker,| Lin Wang,⊥
Matthew E. McCarroll,⊥ Gabor Patonay,X and Isiah M. Warner*,†
Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803, Department of Chemistry,
Winston-Salem State University, Winston-Salem, North Carolina 27110, Department of Chemistry, Nanoscience and
Nanotechnology Institute and the Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242,
Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, Department of Chemistry
and Biochemistry, Southern Illinois University, Carbondale, Illinois 62901-4409, and Department of Chemistry, Georgia
State University, Atlanta, Georgia 30302
Review Contents
Books, Reviews, and Chapters of General Interest
General Instrumentation
Laser-Based Techniques
Sensors
Sample Preparation, Quenching, and Related
Phenomena
Data Reduction
Organized Media
Low-Temperature Luminescence
Total Luminescence and Synchronous Excitation
Spectroscopies and Related Techniques
Solid Surface Luminescence
Luminescence in Chromatography, Electrophoresis,
and Flow Systems
Dynamic Luminescence Measurements
Fluorescence Polarization, Molecular Dynamics, and
Related Phenomena
Chemiluminescence
Near-Infrared Fluorescence
Luminescence Techniques in Biological and Clinical
Analysis
Reagents and Probes
Literature Cited
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This review covers the 2 year period since our last review (1),
from January 2006 through December 2007. A computer search
of Chemical Abstracts provided most of the references for this
review. A search for documents written in English containing the
terms “fluorescence or phosphorescence or chemiluminescence”
published in 2006–2007 resulted in excess of 96 000 hits. An initial
screening reduced this number to approximately 13 000 publications that were considered for inclusion in this review. Key word
searches of this subset provided subtopics of manageable size.
Other citations were found through individual searches by the
various authors who wrote a particular section of this review. In
an effort to more effectively accomplish this goal, we have included
authors who are experts in the various subtopics of this review.
* To whom correspondence should be addressed.
†
Louisiana State University.
‡
Winston-Salem State University.
§
University of Iowa.
|
Oak Ridge National Laboratory.
⊥
Southern Illinois University.
X
Georgia State University.
10.1021/ac800749v CCC: $40.75 2008 American Chemical Society
Published on Web 05/22/2008
Coverage is limited to articles that describe new developments
in the theory and practice of molecular luminescence for chemical
analysis in the ultraviolet, visible, and near-infrared region. In
general, citations are limited to journal articles and do not include
patents, proceedings, reports, and dissertations. Citations may be
duplicated between sections due to articles with contents that span
several topics. However, in an effort to reduce the length of this
review, we have attempted to limit this kind of duplication.
We are not able to provide extensive coverage of all developments of relevance to the extremely broad field of molecular
fluorescence, phosphorescence, and chemiluminescence. Instead,
we have focused on important advances of general interest and
relevance to the field of analytical chemistry, rather than extensions of previous advances. In addition, we have attempted to
balance inclusion of a sufficient number of highly relevant, highimpact references to adequately survey the field with sufficient
description of individual citations for better clarification. If you
feel that we have omitted an important article published during
the above referenced time period, please forward the reference
to one of us and we will be certain to consider it for the next
review.
BOOKS, REVIEWS, AND CHAPTERS OF
GENERAL INTEREST
There were numerous review articles and book chapters
discussing the use and application of luminescence techniques
in the last 2 years. Of particular interest was the publication of
the third edition of Lakowicz’s classic reference, Principles of
Fluorescence Spectroscopy (2). The full color 954 page text has been
updated to include recent results from the literature and the
addition of new chapters including novel fluorophores, single
molecule detection, fluorescence correlation spectroscopy, and
radiative decay engineering. Also appearing during the review
period was the third edition of the book series Reviews in
Fluorescence (3) edited by Geddes and Lakowicz. This compilation
of invited reviews covered a wide range of topics and current
trends. The same authors also edited the 2006 (4) and 2007 (5)
editions of Who’s Who in Fluorescence which provided the names,
contact information, and a brief description of the specialties of
researchers working in the field. Also appearing during the review
period was Berberan-Santos’s Fluorescence of Supermolecules,
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
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Polymers, and Nanosystems (6), the fourth volume in Springer’s
Series on Fluorescence. The reference emphasized fluorescence
of artificial and biological nanosystems, single molecules, polymers, nanoparticles, and nanotubes and also covered fluorescence
microscopy and fluorescence correlation spectroscopy. The 11th
volume of the Topics in Fluorescence Spectroscopy series, Glucose
Sensing (7), edited by Geddes and Lakowicz, covered the emerging area of noninvasive and continuous methods of glucose
monitoring. Didenko edited Fluorescence Energy Transfer Nucleic
Acid Probes: Designs and Protocols (8), the first comprehensive
review of energy transfer nucleic acid probes. The Handbook of
Single Molecule Fluorescence Spectroscopy (9) was also published
during this review period. Emphasis was placed on the practical
aspects of achieving single molecule resolution, data analysis, and
applications in biophysics.
A large number of informative review articles were published
during the review period. Coverage here is limited to a small
number of broad reviews which are likely to be of general interest.
Many reviews focusing on more narrow topics are included
through the various sections of this review. In his review of new
directions in single molecule imaging and analysis, Moerner noted
the recent expansion of this area and summarized emerging areas
such as single molecule based superresolution imaging and single
molecule trapping (10). Tsien and colleagues reviewed the
benefits and limitations of newly developed fluorescent probes
used to study proteins (11). The application of single molecule
fluorescence to the study of protein folding and conformational
dynamics was also reviewed (12). Another review focused on the
benefits and limitations of the major classes of fluorophores used
in Förster or fluorescence resonance energy transfer (FRET) (13).
A critical review, with representative examples, of fluorescent
materials for chemical sensing which employ various chemical
approaches in combination with a variety of materials has also
appeared (14). The use of quantum dots in chemical and
biochemical sensing (15) and the development of fluorescent
core/shell silica nanoparticles showing promise as “lab on a
particle” architectures (16) were also reviewed.
Useful reviews discussing chemiluminescence and phosphorescence also appeared in the literature. For example, a review
with 204 references has covered the recent advances in chemiluminescence published between January 2004 and October 2006
(17). Diaz-Garcia et al. have noted the recent increased interest
in and reviewed the emerging applications of room temperature
phosphorescence in areas such as medicine, geological dating,
and forensics (18).
GENERAL INSTRUMENTATION
Many prototype instruments as well as improvements to
existing instruments were reported during this review period.
Significant advances are achieved with developments of new light
sources, detectors, and methods of data processing. Several
prototype instruments were reported with only a small number
of examples discussed below. Many interesting reports cannot
be discussed due to space limitations, although several other
instrumental advances may be found in other sections of this
review.
In the area of sensors, Valledor et al. discussed the design
and construction of a prototype fiber-optic system using low-cost
optoelectronics for oxygen sensing based on dual phase-shift
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Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
measurements in the frequency domain (19). Bromage et al.
developed a real-time biosensor for detection of trace levels of
trinitrotoluene in aquatic environments (20). A highly specific
monoclonal antibody was coupled with a prototype fluorescencebased detector system. Many instrumental advances were reported
in the area of chromatography, electrophoresis, and flow systems.
One such example is a cam-based scanner as an alternative
approach to detection in capillary array electrophoresis (21). A
prototype instrument was reported to have a constant-velocity
scanning distance similar to 10 mm, a scanning frequency of 3
Hz, and a duty cycle of similar to 70%. We also note that CasadoTerrones et al. compared the performance of a commercial
capillary electrophoresis system using an argon ion laser as the
excitation source with a homemade device based on an inexpensive blue-light-emitting diode (LED) and a charge-coupled device
(CCD) (22). Several examples of portable instrumentation were
found in the areas of biological, clinical, or diagnostic imaging.
For example, Cottrel et al. described a portable instrument that
integrated irradiation with fluorescence and reflectance spectroscopies during clinical photodynamic therapy of cutaneous
disease (23). In another example, Jayachandran et al. reported
the design and development of a hand-held optical probe for
diagnostic imaging (24). This latter design overcame limitations
such as patient comfort and instrument portability by employing
a unique hand-held optical probe designed for simultaneous
multiple point illumination and collection with a curved probe head
that allows flexible imaging of tissue curvatures. Another area
where portable instruments were reported was in the area of rapid
point-of-analysis DNA typing. Mathies and co-workers report an
integrated portable polymerase chain reaction-capillary electrophoresis microsystem. The feasibility of performing forensic
analysis of mass disaster samples or of individuals at a security
checkpoint was established through analysis of real-world oral
swabs and human bone extracts from case evidence (25).
A continuing trend involved both researchers and instrument
manufacturers adapting hardware and/or implementing commercially available instrumentation to better suit the researcher’s
needs. For example, Marwani et al. used a commercially available
frequency domain instrument but collected data via segmentation
before recombining the data sets for analysis in an effort to
address photobleaching and changing fractional contributions
within a multicomponent system, without the need for flow cells
or relatively complex multifrequency instrumentation (26). As an
example of hardware modifications, Dumke et al. described the
reversible modification of a commercial capillary electrophoresis
(CE) instrument (HP 3D-CE or Agilent G1602A) for chemiluminescence detection involving interchanging the deuterium lamp
used for standard absorbance detection with a sidearm photomultiplier tube in the lamp housing (27). Kraikivski et al.
described a complete configuration incorporating both short- and
long-working distance optical trapping configurations into a single
commercially available Zeiss Axiovert 200 M microscope (28).
Manufacturers also improved their commercially available instruments in an effort to meet researchers’ specific needs. As an
example, the NanoLog spectrofluorometer was specially optimized
for recording near-IR fluorescence from nanoparticles and is
reported to offer a number of improvements over the previous
versions (29).
Many developments in the area of detectors have been
reported. A few interesting applications of camera-based and diodebased detectors are discussed below. Wohland and co-workers
reported electron multiplying charge-coupled device camera-based
fluorescence correlation spectroscopy (FCS) (30). The camerabased system allowed multiplexing of FCS measurements but had
a limited time resolution of 4 ms as compared to 0.1-0.2 µs for
instruments using avalanche photodiodes. Rech et al. discussed
the advantages of planar epitaxial silicon single-photon avalanche
diodes (SPADs) as compared to other detectors such as photomultiplier tubes (PMTs) using microchip CE with laser induced
fluorescence (LIF) detection as an example (31). They noted that
PMTs are bulky and/or costly and delicate while SPADs combined
advantages such as small size, ruggedness, low power consumption, and low cost with sensitivity that was better than that of
PMTs.
Detectors for single molecule fluorescence imaging and
spectroscopy were recently reviewed by Weiss and co-workers,
with an emphasis on the required performance of such detectors,
as well as the current state of the art and future developments of
single-photon counting detectors (32). Finkelstein et al. discussed
the performance tradeoffs of single-photon avalanche diode
miniaturization, noting that the performance of compact SPADs
will benefit applications such as high resolution fluorescencelifetime imaging among others (33).
Advances in light sources and methods to direct the light to
or scan the light across a sample continue to improve analytical
measurements. Zeng et al. reported that the use of a prism for
simultaneous compensation of spatial and temporal dispersion
from acousto-optical deflectors used in two-dimensional scanning
improved the signal intensity of two-photon fluorescence microscopy by similar to 15-fold as compared to an uncompensated
scanner (34). Temporal resolution is a challenge for scanning
systems. Wolleschensky et al. reported high-speed confocal
imaging with a novel line scanning microscope capable of
acquisition speeds of 100 frames per second at 512 × 512 pixels
(35). A commercial system based on this concept has been
realized by Carl Zeiss (LSM 5 LIVE). The use of diode light
sources to replace conventional scanning has also been reported.
Ren et al. used a program controlled organic LED array as a
spatial-scanning light source in a whole column fluorescence
imaging application, thus allowing a PMT rather than a CCD
detector to be used without the need for lenses, fibers, or other
mechanical components in the system (36). Poher et al. described
optical sectioning microscopes with no moving parts based on a
microstripe array LED (37). Advances in the use of high power
LEDs continued to be reported. For example, Moser et al.
substituted ultrabright LEDs for conventional excitation sources
in fluorescence microscopy using filter cubes with built-in LEDs
(38). One benefit of the LED system was lifetime imaging without
the need for image intensification. Birch and co-workers described
a 265 nm pulsed LED enabling fluorescence decay of weakly
emitting phenylalanine to be routinely measured in dilute solution
(39). Lucy and co-workers observed that it is not trivial to use
the greater light power provided by new high power LEDs (40).
The large emitting area and highly divergent beam presented a
classic problem in optics where one must balance light collection
efficiency with the size of the focused light spot. The authors
chose collection efficiency and reported low-picomolar limits of
detection in a flow cell.
Another area relevant to general instrumentation which received increased attention is standardization of fluorescence
measurements. Resch-Genger and co-workers developed a set of
traceable fluorescence standards providing the basis for improved
comparability of fluorescence measurements and eventual standardization (41). The Calibration Kit linked fluorescence measurements to the spectral radiance scale in the spectral range of
300-770 nm. The National Institute of Standards and Technology
(NIST) responded to the need for fluorometer qualification and
method validation required for quantitative measurements by
reporting a method to qualify fluorescence spectrometers for
measuring “true” fluorescence spectra (42). In related work, a
multinational collection of nine laboratories using both singlephoton timing and multifrequency phase and modulation fluorometry instruments reported a series of fluorophores with singleexponential fluorescence decays in liquid solution at 20 °C (43).
Lifetimes estimated by both approaches were in agreement, and
the standards were suitable for calibration or testing the resolution
of both time- and frequency-domain instrumentation. Calibration
of a wide-field frequency-domain fluorescence lifetime microscope
(44), the emission light path of confocal microscopes (45), and
the probe volume in fluorescence correlation spectroscopy (46)
has also been reported. Comparisons of FRET measurements
based on different imaging modalities (47) and FRET standards
designed for use and exchange between laboratories (48) appeared during this review period. Finally, calibration standards
for multicenter clinical trials of fluorescence spectroscopy for in
vivo diagnosis (49) and instrumentation as a source of variability
in detecting cervical neoplasia (50) has been discussed.
LASER-BASED TECHNIQUES
Of general interest to this topic is a recent review by Smith.
The author described the reluctance of analytical chemists to
embrace lasers and their increasing acceptance over the past 25
years. The review noted that the use of lasers in commercial
analytical instrumentation was not always widespread. However,
one area in which lasers have found utility is in a wide range of
new spectroscopic microscopies (51). Laser-based techniques
such as single molecule detection, optical tweezers and traps, FCS,
multiphoton excitation, and fluorescence lifetime and confocal
microscopies rely heavily on the high irradiance of laser sources.
These techniques are becoming more routinely used and several
have been commercialized and are widely applied in fields such
as the life sciences. Advances continue to be reported even as
the use of these techniques as tools to investigate complex
problems have become increasingly more common.
Improved lasing media for dye lasers continues to be an area
of interest. Ray et al. have investigated the possibility of employing
the photothermal characteristics of water as a solvent for dye
lasers (52). Their results suggest that binary solvents composed
of water and about 18% to 25% n-propanol produced similar
efficiency, better photochemical stability, and superior thermooptic properties than ethanol alone. Garcia-Moreno et al. synthesized and studied polymerizable analogues of the borondipyrromethene (BODIPY) dye PM567 copolymerized with methyl
methacrylate in search of more efficient and photostable solidstate dye lasers (53). They reported the highest photostability
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
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achieved to date for solid-state lasers based on organic polymeric
materials doped with laser dyes.
Several examples of supercontinuum light source based imaging systems have been reported. For example, Kano et al. obtained
both vibrational and two-photon excitation fluorescence images
of living cells simultaneously at different wavelength using a
supercontinuum light source (54). The supercontinuum allowed
multinonlinear optical imaging through two different nonlinear
optical processes. A confocal microscope using a supercontinuum
laser excitation source and a custom-built spectrometer for
detection was reported by Frank et al. (55). The system allowed
collection of fluorescence excitation and emission spectra for each
location in a 3D confocal image.
Single molecule detection continued to provide valuable
information. For example, Seeger and Li demonstrated the labelfree detection of single protein molecules using deep UV fluorescence lifetime microscopy (56). A time-resolved single photon
counting method and fluorescence correlation spectroscopy were
employed. Intrinsic fluorescence upon one-photon excitation at
266 nm was useful for identification of biological macromolecules.
The use of single molecule fluorescence to examine molecular
interactions in various systems is becoming more common.
Pappas et al. have reviewed recent applications of single molecule
detection investigating biomolecular interactions (57). The focus
was placed on instrumentation and tools such as anisotropy and
resonance-energy transfer. Single molecule microscopy was used
in conjunction with interferometric detection of single gold
nanoparticles and fluorescence lifetime measurements to investigate modification of the fluorescence decay rate of single dye
molecules tethered at various distances from a nanoparticle (58).
Nanoparticle induced lifetime modification served as a nanoscopic
ruler at distances beyond the upper limit of FRET. Recently, Lee
et al. introduced three-color alternating-laser excitation (3c-ALEX),
a FRET technique that measured up to three intramolecular
distances and complex interaction stoichiometries of single
molecules in solution (59). Widengren and co-workers recently
discussed strategies to chemically retard dye photobleaching
through the use of antifading compounds in ultrasensitive fluorescence measurements such as FCS, fluorescence-based confocal
single molecule detection, and related techniques (60).
Several papers reported the development and application of
optical tweezers and traps. One example applied FCS to the
measurement of the local heating under laser trapping condition
in the presence of a near-infrared laser beam (61). The relationship
between the temperature rise and the incident laser power was
determined. In other work, Li et al. reported single molecule
fluorescence studies of multiple fluorophore-labeled antibodies in
solution (62). Trapping was observed at laser powers below 1 mW
with resonant excitation. The authors noted that selective resonance trapping may allow sorting and manipulation of biomolecules and complexes. Merenda and co-workers used an array of
high numerical aperture parabolic micromirrors to generate
multiple optical tweezers and trap particles in 3D within a fluidic
device (63). The micromirrors could simultaneously collect
fluorescence from the trapped particles. This approach offered a
simple and efficient solution for miniaturized optical traps in
laboratory-on-a-chip devices.
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Many new methods continued to be reported that helped
fluorescence correlation spectroscopy to meet the somewhat
stringent requirements imposed by the technique (i.e., high rate
of photon detection per molecule from a relatively small number
of molecules). Generally, very low fluorophore concentrations are
necessary. This does not pose a problem for in vitro measurements. However, micromolar concentrations are often encountered
in fields such as biology. Alternatives to conventional confocal
geometries are required to further confine the probe volume.
Examples of FCS using a subwavelength sized aperture (64) in a
surface plasmon coupled emission microscope (65) and utilizing
single-mode optical fiber (66) were reported during the review
period. Additional advances included a newly developed singleelement aspheric objective lens that reduced the cost of FCS
instruments and improved biomolecule quantification precision
(67) and a prism-based multicolor instrument that offered high
optical stability and no focal volume mismatch for the multicolor
detection of molecular dynamics (68). A new distributed algorithm
for multi-τ autocorrelation was also reported to reduce the memory
requirements associated with accessing the large time-domain data
records generated in FCS experiments (69). Schwille and coworkers observed that the dominant effects limiting the quality
of two-photon fluorescence correlation measurements were inherent properties of the dye system such as bleaching and saturation
(70). The authors noted that elaborate optimization of temporal
and spectral laser pulse width through introduction of pulse
stretchers in the beam path may be less critical than previously
believed. Wiseman and co-workers extensively investigated the
accuracy and precision of temporal image correlation spectroscopy
as related to sampling effects, noise, and photobleaching (71).
Photobleaching of the fluorophore was shown to cause a consistent overestimation of diffusion coefficients and flow rates and a
severe underestimation of number densities. A bleaching correction equation was developed to remove these biases.
Advances in multiphoton excited fluorescence continue to be
reported. Many systems that combined multiphoton imaging with
other imaging modes were described. For example, Rothstein et
al. reported two-photon excitation fluorescence and backscatteredsecond harmonic generation microscopy measurements in intact
animals (72). Quality images were routinely collected from both
the peripheral and body cavity organs. Joo et al. combined spectraldomain optical coherence phase and multiphoton microscopy (73).
A novel multifocal multiphoton microscope was reported to
provide simultaneous time- and spectrum-resolved fluorescence
microscopy (74). Acquisition of five-dimensional data combing
lifetime and spectral resolutions in biological imaging was
demonstrated. Other reports included a demonstration by Bird
et al. of the effectiveness of a photonic crystal fiber as a means of
optimizing the temporal response in multichannel two-photon
fluorescence microscopy (75). Their findings are pertinent to
other systems that use a multimode optical fiber in lifetime
measurements. Ragan and co-workers reported 3D particle tracking using a two-photon microscope (76). McConnell reported a
greater than 3-fold increase in the penetration depth of multiphoton excitation laser scanning microscopy through the use of a
passive predispersion compensation system (77). Systems allowing imaging at multiple focal planes were also described. Bahlmann et al. reported a high-speed multifocal multiphoton micro-
scope with a frame rate of 640 Hz (78). A two-photon scanning
microscope capable of simultaneous imaging of three or more
focal planes was described by Amir et al. (79). Haeberle and Simon
proposed a simple technique, based on laterally interfering beams,
to improve the lateral resolution in confocal fluorescence microscopy (80). It was shown that use of two-color two-photon excitation
could permit resolution of 60 nm. The previous reference is an
example of an emerging area that has seen rapid progress in
recent years. The many advances in far-field fluorescence imaging
techniques providing subdiffraction limit resolution cannot be
adequately surveyed in the space provided. However, two recent
reviews have examined this emerging field. Rice outlined developments in ultrahigh resolution far-field florescence methods with
emphasis on application of these techniques to biology (81). Hell
discussed the physical concepts that have pushed fluorescence
microscopy to the nanoscale (82). The author avoided discussing
technical aspects in great detail but instead focused on how
fluorescence nanoscopy concepts to date have relied on “bright”
and “dark” states of the fluorescenct molecule to break Abbe’s
diffraction barrier.
SENSORS
Many novel fluorescence sensors for various analytes were
reported during the review period. An area continuing to receive
attention was the detection of warfare agents. Simonian and coworkers described a fluorescent-based biosensor for the detection
of organophosphate pesticides and chemical warfare agents (83)
and modified an array biosensor unit developed at the Naval
Research Laboratories for enzyme-based measurements with the
potential for direct detection of organophosphates (84). Other
reports included fluorescent organometallic sensors for the
detection of chemical-warfare-agent mimics (85) and a small
molecule photoinduced electron transfer (PET)-based sensor that
provided an optical response to a nerve agent mimic (86). Anslyn
and co-workers described a fast PET-based “off-on” response to
chemical warfare simulants upon phosphorylation of a coumarin
oximate (87).
Nguyen and Anslyn reviewed indicator displacement assays
(IDAs), which is a popular method to convert almost any synthetic
receptor into an optical sensor (88). Singaram and co-workers
described the design and use of boronic acid appended bipyridinium salts as receptors in an IDA-based sensor array to
differentiate saccharides in aqueous solution at neutral pH (89).
The same group was also active in the area of glucose sensing
including reports on the use of quantum dots with boronic acid
substituted viologens to sense glucose (90) and the simultaneous
use of multiple fluorescent reporter dyes for glucose sensing in
aqueous solution (91). In other work, the Strongin group
discussed the stereochemical and regiochemical trends in the
selective detection of saccharides and presented a boronic acidfunctionalized rhodamine derivative which displayed an unprecedented degree of colorimetric and fluorimetric selectivity for
ribose and ribose derivatives (92). The same group also described
the used of simple water-soluble lanthanum and europium
complexes as indicators for neutral sugars and cancer biomarkers
(93).
Detection of thiols continued to be an active area of examination. For example, Huang and co-workers were active in the area
of cysteine/homocysteine sensing. Reports included a selective
phosphorescence chemosensor for homocysteine based on an
iridium(III) complex (94) and a novel Y-shaped fluorophore with
potential as a two-photon excited fluorescent sensor for cysteine
and homocysteine (95). The same group also described a turnon sensor for cysteine/homocysteine with excitation in the visible
region (96). Use of the sensor for the imaging of biological
samples was demonstrated.
Because of its role in regulating a variety of biological
processes, detection of nitric oxide (NO) is of recognized
importance. Zguris and Pishko discussed a NO sensor based upon
4-amino-5-methylamino-2′,7′-difluorofluorescein entrapped in a
poly(ethylene glycol) hydrogel microstructure prepared by photolithography (97). Sweedler and co-workers used a specific
enzymatic reaction to eliminate the confounding effect of ascorbic
acid on diaminofluorescein quantitation of NO and then used CE
with LIF detection to distinguish the various reaction products
(98). The simple methodology allowed NO to be measured in
single cells without detectable interference from other compounds.
Lim and Lippard reviewed metal-based turn-on probes developed
by the Lippard laboratory for the detection of NO (99).
Schroder et al. described a hybrid time-resolved sensor based
upon a lipophilic fluorescein derivative (lifetime similar to 5 ns)
and platinum(II) mesotetrakis(pentafluorophenyl)porphyrin (lifetime similar to 70 µs in the absence of a quencher) immobilized
in a hydrogel matrix for the simultaneous mapping of pH and pO2
(100). Wolfbeis and co-workers reported fiber-optic microsensors
for the simultaneous sensing of oxygen and pH or oxygen and
temperature (101). The sensor utilized luminescent microbeads
whose decay time and/or luminescence intensity responded to
changes in the respective analytes. Valeur and co-workers reported
the photophysics of a series of efficient fluorescent pH probes
for dual-emission-wavelength measurements in aqueous solutions
(102).
Many assays and sensor systems based on biological recognition elements such as antibodies, aptamers, enzymes, etc. are often
expensive and unstable. Bright and co-workers reviewed the
development of molecularly imprinted organic and inorganic
polymers as possible replacements for biorecognition elements
(103) and described a biomolecule-less biomolecule sensor that
relied upon molecular imprinting of sol-gel-derived xerogels with
the selective installation of a luminescent reporter molecule
directly within the molecularly imprinted site (104).
Fluorescent conjugated polymers have shown great potential
as signal transduction materials in chemical sensors. Swager and
co-workers recently reviewed chemical sensors based on amplifying fluorescent conjugated polymers (105). Nesterov and coworkers described a general approach to cross-linked molecularly
imprinted fluorescent conjugated polymer (MICP) materials and
prepared an MICP material for the detection of 2,4,6-trinitrotoluene
and related nitroaromatic compounds (106).
A large number of papers reporting sensors for various metal
cations appeared during the review period. Only a small number
of papers with an emphasis on turn-on and ratiometric modes of
detection are described here. Fan and Jones prepared a highly
selective and sensitive turn-on sensor for iron cations based on a
transition metal derivatized conjugated polymer (107). Van Dongen et al. described ratiometric fluorescent sensor proteins and
tuned their affinity toward Zn(II) in the pico- to femtomolar range
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4555
using a series of flexible peptide linkers (108). Komatsu et al.
developed an iminocoumarin-based zinc sensor for ratiometric
fluorescence imaging of neuronal zinc (109). Zeng et al. synthesized a new turn-on fluorescent chemosensor for imaging labile
Cu(I) in living cells (110). Yang et al. synthesized a new
naphthalene derivative with two urea groups for ratiometric Cu(II)
detection (111). The Lippard laboratory described a red-emitting
seminaphthofluorescein-based turn-on and single-excitation dualemission ratiometric Hg(II) sensor for use in aqueous solution
(112).
Compared to cations, the sensing of anions has generally been
more difficult to achieve; however, research in this area has
increased. Some examples reported during the review included a
simple, highly selective, neutral, fluorescent sensor for fluoride
anions (113) and the design of a fluorescence turn-on sensor array
for phosphates such as AMP and ATP in blood serum (114). The
Gunnlaugsson group has reviewed luminescent and colorimetric
anion sensors developed in their laboratory based on hydrogen
bonding in organic or aqueous solvents (115).
SAMPLE PREPARATION, QUENCHING, AND
RELATED PHENOMENA
Quenching techniques continue to be an active area of research
during this review period. Several reports discussed quenching
in the nano regime. Cognet observed the stepwise quenching of
mobile exciton fluorescence in carbon nanotubes after exposure
to acid, base, or diazonium reactants using near-infrared photoluminescence microscopy (116). Their analysis revealed a 90 nm
exciton diffusional range independent of nanotubes structure and
that each exciton visited about 10 000 atomic sites during its
lifetime resulting in highly efficient sensing of local physical and
chemical perturbations. Schneider et al. fabricated fluorescent
core/shell nanoparticles based on 13 nm gold cores and layerby-layer assembly of fluorescently labeled polymer corona layers
at various distances from the metal core (117). The quenching
behavior of the system was strongly distance-dependent. Strouse
and co-workers used fluorescent lifetime quenching of molecular
dyes at discrete distances from 1.5 nm gold nanoparticles to
demonstrate that the quenching behavior was constant with 1/d4
separation distance dependence and that energy transfer to the
metal surface was the dominant quenching mechanism (118).
Pons et al. monitored the photoluminescence quenching of
CdSe-ZnS quantum dots (QDs) by gold nanoparticle acceptors
at center-to-center distances in the range of 50-200 Å using steady
state and time-resolved measurements (119). The authors indicated that the nonradiative quenching was due to long-distance
dipole-metal interactions extending significantly beyond the
classical Förster range. In other work, Laferriere et al. demonstrated that the quenching of QD luminescence by nitroxides was
extremely nonlinear and dependent on particle size (120). In an
effort to gain the knowledge needed to design efficient QD organic
optoelectronic devices, Huang et al. investigated the bias-induced
photoluminescence quenching of single QDs embedded in organic
semiconductors, noting the importance of chemical compatibility
between the QD and its surroundings (121).
A wide variety of sensing platforms based on fluorescence
quenching have also been reported. Examples include a fluorescence quenching based sensor for selective detection of dopamine,
levodopa, adrenaline, and catechol utilizing phosphate-modified
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TiO2 nanoparticles (122), a protein cavity mimicking chemosensor
in which the position of the fluorescent anthracene moiety
modulated the Cu(II) induced emission properties from quenching
to enhancement (123), and an optical sensor for 2,6-dinitrophenol
based on fluorescence quenching of a novel functional polymer
(124). Many high profile examples of quenching based systems
employing conjugated polymers have also been reported. Examples include reports of anion-induced colorimetric response and
amplified fluorescence quenching in dipyrrolylquinoxaline-containing conjugated polymers (125) and the use of fluorescence
quenching of conjugated polymers for the detection of Diels-Alder
reactions (126). Muller et al. have investigated the role of exciton
hopping and direct energy transfer in the efficient quenching of
conjugated polyelectrolytes (127). Liao and Swager have quantified the amplified quenching in a conjugated polymer microsphere
system in response to methyl viologen and a naphthyl-functionalized viologen (128).
Improvements have also been reported in the area of immunoassays. Ramanavicius et al. have developed a new approach to
increasing the selectivity of immunosensors by use of conducting
polymer-based fluorescence quenching (129). Ao et al. have
developed a highly specific immunoassay system for antigen
detection based on fluorescence quenching of fluorescein isothiocyanate caused by gold nanoparticles coated with monoclonal
antibody (130). Baker et al. have reported a fluorescence quenching immunoassay performed in an ionic liquid (131).
Advances in the use of fluorescence quenching in DNA and
RNA detection schemes continue to be widely reported. Abe and
Kool have described the use of quenched autoligating FRET
probes in the flow cytometric detection of mRNAs in live human
cells (132). Brennan and co-workers thoroughly investigated the
quenching of fluorophore-labeled DNA oligonucleotides by divalent metal ions in an effort to develop general principles that will
improve future application of signaling DNA aptamers and
deoxyribozymes as biosensing probes (133). Bulygin and Milgrom
used fluorescence quenching to investigate nucleotide binding to
the catalytic sites of Escherichia coli βY331W-F1-ATPase (134).
Previous to this report, most studies had been performed in the
presence of ∼20 mM sulfate. This study reported that in the
absence of sulfate, the nucleotide concentration dependence of
fluorescence quenching induced by ADP, ATP, and MgADP was
biphasic.
DATA REDUCTION
The application of various data reduction techniques involving
the use of linear regression modeling such as partial least-squares
(PLS), principal components regression (PCR), and multilinear
regression (MLR) for fluorescence data analysis and multivariate
calibration continues to be of significant interest during this review
period. Consequently, several papers have reported the utility and
practical application of linear regression modeling for the investigation of molecules of industrial, pharmaceutical, biomedical,
clinical, and environmental interest. For example, Yang and Li
reported the use of regression modeling for simultaneous detection and quantification of two species of foodborne pathogenic
bacteria using quantum dots as fluorescence labels (135). In
another study, the advantage of PLS over a multivariate curve
resolution (MCR) technique for signal deconvolution in multiplexed analyses for simultaneous fluorophore detection was
demonstrated (136). Multivariate calibration involving the use of
PLS regression analysis of fluorescence emission for the analysis
and determination of enantiomeric composition of molecules of
pharmaceutical interest were also reported (137–140).
In addition to linear PLS regression, a second-order multivariate calibration technique involving the use of unfolded-partial leastsquares with residual bilinearization (U-PLS/RBL) (141, 142) and
a novel third-order calibration approach, multiway-partial leastsquares with residual trilinearization (N-PLS/RTL) (143) for
chemical analysis were developed. According to the authors, as
compared with linear regression, the use of a second and a third
order regression calibration was advantageous, with better prediction ability. Other interesting articles on the use and applications
of a second- and a third-order multivariate analysis were recently
reviewed by Escandar et al. (144).
Many research articles have also reported the use of a multilinear
regression (MLR), especially in combination with other data reduction techniques for multivariate calibration. Aghamohammadi et al.
have demonstrated the practical application of MLR for accurate
determination of aflatoxin B-1 in pistachio samples at part per billion
concentrations (145). In addition, the utility of MLR when combined
with a genetic algorithm for a multiexponential fluorescence decay
surface study (146) was reported. Furthermore, the use of MLR in
conjunction with successive projections algorithm (MLR-SPA) for
simultaneous and direct spectrophotometric determination of five
phenolic compounds in seawater (147) was published. Compared
with PLS regression, the use of MLR-SPA was reported to have better
analytical performance, with potentially better resolution of complex
analytical data.
The application of the fluorescence excitation-emission matrix
(EEM) in combination with parallel factor analysis (PARAFAC)
has become increasingly important for the characterization and
qualitative analysis of complex systems. Hence, many researchers
have reported the utility of EEM-PARAFAC technique for investigation of a wide range of complex mixtures during the review
period. For example, Bosco et al. have investigated the photocatalytic degradation of phenol (148) and photodegradation
kinetics of dibenz[a,h]anthracene, benz[a]anthracene, benz[a]pyrene, and benz[k]fluorantene polycyclic aromatic hydrocarbons
(PAHs) in aqueous suspensions using EEM-PARAFAC (149).
With the use of this approach, the spectra of the photodegrading
species were successfully resolved, affording accurate quantification of the PAHs concentration during the photodegradation
process. The practical application of the EEM-PARAFAC techniques in environmental studies for characterization of dissolved
organic matter in the ecosystem were also demonstrated (150, 151).
Other important applications involving the use of the EEMPARAFAC approach included its use to unravel the complexation
mechanism and binding mode of DNA with ternary copper(II)
complexes (152) as well as the use of EEM-PARAFAC combined
with PLS regression for qualitative and quantitative analysis of
cell density evolution in biological samples (153).
Many research papers on the use of principal components
analysis (PCA), linear discriminant analysis (LDA), artificial
neutral network (AAN), K-nearest neighbor (K-NN), and soft
independent model of class analogy (SIMCA) for effective classification and pattern recognition of wide range of complex
fluorescence data have been reported during this review period.
Zhou et al. reported the use of PCA for pattern recognition in a
protein-detecting array based on porphyrins containing peripheral
amino acids as protein surface receptors to distinguish between
the metal and nonmetal-containing proteins (154). Kunnil et al.
employed PCA in combination with cluster analysis of fluorescence
emission to accurately differentiate between Bacillus globigii
spores from the other species of Bacillus spores (B. cereus, B.
popilliae, and B. thuringiensis) (155). In addition, there was a
report of application of PCA in food analysis for effective monitoring of the oxidation pattern and quality of semihard cheeses (156).
In another interesting study, Rowe and Neal developed a novel
method involving the use of PCA and frequency-domain fluorescence for investigation of the photokinetic property of prodan and
laurdan in large unilamellar vesicles (157). Application of other
important classification techniques such as K-nearest (158, 159),
artificial neutral network (160, 161), linear discriminant analysis
(162), soft independent model of class analogy (163), and
extended canonical variates analysis (164) in fluorescence studies
for effective pattern recognition and accurate classification in
various research studies were also demonstrated.
Various other data analysis and data reduction techniques,
particularly, in fluorescence imaging and single molecule detection
were also developed. Clegg and co-workers reported a method
for fitting frequency-domain lifetime images in the presence of
photobleaching (165). The method improved the speed of current
numerical techniques up to 1000-fold and was fast enough to
analyze images in real time. The use of multiparameter fluorescence detection (MFD) imaging for simultaneous investigation
of changes in fundamental anisotropy, fluorescence lifetime,
fluorescence intensity, time, excitation spectrum, fluorescence
spectrum, fluorescence quantum yield, and distance between
fluorophores in real time (166) was demonstrated. In another
study, MFD was employed for the detection and quantification of
labeled- oligonucleotides species in solution (167). Jung and Van
Orden demonstrated the application of multiparameter fluorescence fluctuation spectroscopy for the investigation of folding of
a dye-quencher labeled DNA hairpin molecule (168).
The practical applications of fluorescence correlation spectroscopy (FCS) and time-correlated single photon counting (TCSPC)
also continues to be of significant analytical interest. Consequently,
many research articles involving the use of FCS and TCSPC for
various applications were published since the last review. For
example, Werner et al. investigated the transition between aciddenatured states and the native structure of cytochrome c from
Saccharomyces cerevisiae using FCS and TCSPC (169). According
to the authors, compared to the use of either FCS or TCSPC alone,
better results were obtained when FCS and TCSPC were used in
combination. Other notable papers demonstrating the utility and
practical application of FCS were those published by Burkhardt
and Schwille (170) and Culbertson et al. (171).
In conclusion, it is apparent that the application and development of new data analysis and data reduction strategies in
fluorescence continues to be of significant interest. It is likely that
many new developments and applications of data reduction will
find practical utility in analytical, biomedical, clinical, and environmental studies as well as in material analysis and in the food
industry for many years to come.
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
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ORGANIZED MEDIA
Organized media is a broad term that describes a wide variety
of systems that can compartmentalize solvent or solutes and
sequester them from the bulk environment. Aaron and co-workers
have reviewed environmental analyses based on luminescence in
organized supramolecular systems such as micellar media and
cyclodextrin (CD) inclusion complexes reported between 1990 and
2005 (172). The Warner laboratory reviewed a selection of studies
performed by the group investigating the properties of CD
host-guest complexes and recent work performed by other
laboratories using CDs in applications such as photochemical
antennas and sensors (173).
Many interesting reports on a wide range of various organized
media have appeared during this review period. Only a small
subset of representative examples can be included in this survey.
Mohanty et al. compared the complexation of neutral red (NR)
with the macrocycle host molecules cucurbit[7]uril (CB[7]) and
β-CD (174). In similar work, Liu et al. demonstrated that β-CD,
calix[4]arene tetrasulfonate (C4AS), and CB[7], supramolecular
hosts possessing different types of cavities, lead to different
complexation-induced fluorescent behaviors of dyes including
acridine red (AR), neutral red (NR), and rhodamine B (RhB)
(175). For C4AS and CB[7] hosts, the complexation stability
constants decreased in the order of NR > AR > RhB, while the
order was reversed for β-CD.
Several reports using CDs in the determination of various
analytes appeared during the review period. Examples included
the use of hydroxypropyl-β-CD enhanced fluorescence quenching
for determination of vitamin B-12 (176) and the determination of
3-hydroxy-2-naphthoic acid in river water by use of its ternary
complex with zirconium(IV) and β-CD (177). Chiral recognition
based upon CD complexation has also been widely reported. In
one such example, Zhang et al. used γ-CD as the chiral selector
in the discrimination of quinine and quinidine (178). Quinine and
quinidine displayed strong room temperature phosphorescence
(RTP) in γ-CD solution upon addition of small amounts of
bromocyclohexane. Different RTP lifetimes indicated a distinct
chiral discrimination for this pair of pseudoenantiomers.
Chiral molecular micelles (MMs) are another example of
organized media used for chiral discrimination. The Warner
laboratories have reported the use of chiral MMs combined with
multivariate regression analysis of spectral data to determine the
enantiomeric composition of fluorescent chiral analytes (179). In
another example, the same group used steady-state fluorescence
anisotropy, capillary electrophoresis, and NMR to investigate the
mechanisms of chiral recognition displayed by four diastereomers
of the chiral MM poly(sodium N-undecanoyl leucylvalinate) (pSULV) for neutral and anionic chiral analytes (180).
Several reports of dendrimers, resorcinarenes, and calixarenes
have appeared during this review period. Representative examples
included the spectroscopic characterization of poly(amidoamine)
dendrimers as selective uptake devices (181), the use of fluorescence resonance energy transfer to probe the dynamic behavior
of resorcinarene capsules at nanomolar concentrations (182), and
an investigation of atropine and cocaine host-guest interactions
with a dansyl amide labeled calix[6]arene (183). The groups of
Tucker and Atwood reported the cocrystallization and encapsulation of a fluorophore with hexameric pyrogallol[4]arene (184).
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Structural and fluorescence studies demonstrated that relatively
small molecules can dramatically change the extended packing
of large robust supramolecular entities.
Investigations of nonionic micellar systems continue to be
reported. Because external probes may affect the property of
interest, Pandey and co-workers have used steady-state and
frequency domain techniques to probe the intrinsic fluorescence
from the phenyl moiety of Triton X-100 in water (185). The
concentration dependent emission and excitation were used to
monitor the presence of micelles, while the decay data were used
to characterize the dynamic parameters of the micelles. In other
work, Pallavicini et al. reported an on-off fluorescence sensor
response which could be transformed into an off-on response
through a change in the lipophilicity of the receptor (186). When
a more lipophilic long chain was used to lipophilize a ligand
residing inside TritonX-100 micelles together with pyrene, an
on-off sensor was obtained. An intermediate chain length resulted
in an off-on response.
Ioffe et al. synthesized a new fluorescent squaraine probe for
the measurement of membrane polarity (187). Moerner and coworkers described a class of dicyanomethylenedihydrofuran
(DCDHF) fluorescent lipid analogues capable of single molecule
imaging of diffusion in the cell membrane of live cells (188). The
authors observed individual molecules of several different DCDHF
lipid analogues diffusing in the plasma membrane of Chinese
hamster ovary cells. In other related work, Hochstrasser and coworkers used single molecule fluorescence confocal microscopy
to probe the association and dissociation reactions of single Nile
Red molecules with a lipid vesicle (189). Nile Red was shown to
be a useful probe of the structural fluctuations and heterogeneity
of membrane structures.
Other related investigations employing techniques such as
fluorescence lifetime imaging and other time-resolved techniques
as well as fluorescence correlation spectroscopy were reported.
Margineanu et al. used a perylene monoimide derivative and
fluorescence lifetime imaging to visualize membrane rafts (190),
and de Almeida et al. combined imaging with microscopic and
macroscopic time-resolved fluorescence in an investigation of lipid
domains and rafts in giant unilamellar vesicles (191). Fluorescence
lifetime correlation spectroscopy was demonstrated to be a
powerful technique in phospholipid bilayer research (192).
Schwille and co-workers investigated the effects of ceramides,
compounds known to influence lipid lateral organization in
biological membranes, on liquid-ordered domains using simultaneous atomic force microscopy and FCS (193). The same group
also studied slow membrane dynamics with continuous wave
scanning FCS (194). In other work, Rhoades et al. demonstrated
that FCS was a powerful tool for the quantitative characterization
of R-synuclein binding to lipid vesicles (195).
Interesting work in the area of protein clusters was also
reported. Sieber et al. used a combination of far-field optical
nanoscopy, biochemistry, fluorescence recovery after photobleaching, and simulations to investigate the anatomy and dynamics of a supramolecular membrane protein cluster (196). The
average diameter of syntaxin clusters was shown to be 50-60 nm
and contain 75 densely crowded syntaxins which freely exchange
with diffusing molecules.
The variety of structures and tunable properties of polymer
thin films and mesoporous materials formed by cooperative selfassembly of surfactants and framework building blocks allow
attractive host systems for a variety of applications. However,
behavior and movement of molecules within these systems are
not fully understood. Single molecule spectroscopy is a useful tool
to investigate these systems. For example, Clifford et al. investigated the blinking behavior of Atto647N, an organic carborhodamine dye, in various polymer matrixes including polynorbornene (Zeonex), poly(vinyl carbazole), and poly(vinyl alcohol)
(197). The diffusion of Nile Red in mesoporous silica thin films
was studied using fluorescence imaging and single-point fluorescence time transients by Higgins and co-workers (198). Bein and
co-workers presented the combination of electron microscopic
mapping and optical single molecule tracking experiments to
investigate the diffusion of single luminescent dye molecules in
mesoporous materials (199). The combination of structural
information provided by TEM and dynamic information from
optical microscopy allowed an understanding of host-guest
interactions not previously possible.
LOW-TEMPERATURE LUMINESCENCE
Many research articles with applications of low-temperature
and related luminescence techniques have been reported during
this review period. In particular, there were considerable efforts
concerning the investigation of metal-enhanced phosphorescence
(MEP) at low temperature. For example, Geddes and his research
group have demonstrated enhancement of phosphorescence
intensity when silver island films (SiFs) are in close proximity to
Rose Bengal at 77 K (200). In a related study, an increase in S-2
emission intensity of azulene on SiFs was reported (201). Practical
application of low-temperature luminescence for the investigation
of photophysical properties of a series of 3,4-ethylenedioxythiophene oligomers (OEDOT) of many repeating units was also
demonstrated (202). Sardar et al. also employed low-temperature
phosphorescence measurements to investigate the complexation
mechanism between human placental ribonuclease inhibitor (hRI)
containing six tryptophan (Trp) residues and bovine pancreatic
ribonuclease A (203).
Several papers also reported the application of low-temperature
single molecule fluorescence measurements. Richter et al. have
reported the use of single molecule fluorescence excitation spectra
at low temperature (1.4 K) for investigations of reaction centerlight-harvesting complexes from Rhodopseudomonas palustris and
the PufX- strain of Rhodobacter sphaeroides (204). Da Como et
al. have demonstrated the application of low-temperature single
molecule fluorescence spectroscopy for the characterization of
one-dimensional crystalline β-phase of polyfluorene nanowires
(205). The practical utility of low-temperature luminescence in
environmental studies was also demonstrated. Yu et al. determined
fluoroquinolones in water samples at part per billion levels by
measuring fluorescence emission and lifetime at low temperature
(206). There was also a report of a unique screening strategy of
polycyclic aromatic hydrocarbons (PAHs) in soil samples by
fluorescence measurements of cryogenic probe at liquid helium
temperature (207). In a related study, Zhang et al. developed a
novel technique involving the use of low-temperature Shpol’skii
effect and nonlinear variable-angle synchronous fluorescence
spectrometry in combination for simultaneous identification and
quantification of PAHs in mixtures (208). It is apparent that the
use of low-temperature luminescence continues to be of significant
interest since the last review. Consequently, considerable efforts
were made in the development of analytical equipment and
instrumentation to enhance the capability and applicability of lowtemperature luminescence techniques in various research areas
(209–211).
TOTAL LUMINESCENCE AND SYNCHRONOUS
EXCITATION SPECTROSCOPIES AND RELATED
TECHNIQUES
The use of total luminescence and synchronous fluorescence
spectroscopy (SFS) continues to be active and exciting research
areas for various applications, ranging from material and food
analysis, quality assurance, DNA, protein and drug analysis to
cancer diagnosis and environmental studies. For example, SFS
was employed for quantitative determination of virgin olive oil
adulteration with sunflower oil (212). According to the authors,
the sunflower oil in virgin olive oil can be detected down to 3.4%
(w/v) in less than 3 min. Deepa et al. used synchronous
fluorescence and excitation-emission spectra to evaluate the
aging and degradation of transformer oil (213). In a related study,
analysis of petroleum products by use of SFS in conjunction with
multivariate analysis has been demonstrated (214). The technique
was reported to be sensitive, capable of detecting 1% contamination
of kerosene in petrol.
SFS has also been widely used for the analysis of biological
samples. Application of SFS for the detection of single-stranded
and double-stranded DNA using methylene blue as a fluorescence
probe has been reported (215). The fluorescence intensity of the
methylene blue probe was observed to be quenched proportionally
to the concentration of DNA in the solution. With the use of this
technique, calf thymus DNA (ctDNA), thermally denatured
ctDNA, and herring sperm DNA (hsDNA) were detected at low
concentrations, with detection limits ranging from 0.04 to 0.11
µmol L-1. In a similar study, Hou et al. demonstrated the use of
SFS for the investigation of human serum albumin (HSA) using
methyl blue as a fluorescence probe (216). Complexation between
the HAS and methyl blue probe at pH 4.1 was reported to
significantly increase the synchronous fluorescence intensity. In
addition, the detection limit of HSA in human serum samples of
0.03 µg mL-1 obtained using synchronous fluorescence scan
analysis was comparable when employed with clinical data. SFS
was also employed for investigation of the interaction between
N-(p-chlorophenyl)-N′-(1-naphthyl) thiourea and serum albumin
(217), and the synchronous fluorescence of a novel functional
organic nanoparticle, dodecyl benzene sulfonic acid sodium salt
(DBSS)-capped nanoanthracene, for protein analysis was reported
(218). This protein analysis technique was found to be highly
reproducible, accurate, sensitive, and reliable, with potential for
practical application.
Many research studies have also demonstrated the practical
utility of SFS for the analysis of molecules of pharmaceutical
interest. For example, Karim et al. reported the use of first
derivative synchronous fluorimetry for a rapid and simultaneous
determination of acetylsalicylic acid and caffeine in a pharmaceutical formulation (219). Pulgarin et al. developed a method using a
derivative matrix isopotential SFS for direct determination of two
anti-inflammatory drugs, diflunisal and salicylic acid, in human
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4559
serum (220). Application of SFS to tissue analysis for early cancer
diagnoses also continues to be of significant biomedical and
clinical interest. In particular, Diagaradjane et al. employed
changes in the synchronous fluorescence property of tryptophan,
collagen, and NADH during a tissue transformation process as
tumor biomarkers to diagnose normal from abnormal tissues in
a mouse skin tumor model (221). In a related study, the use of
synchronous fluorescence imaging for tissue diagnosis in vivo in
a mouse skin model was also developed by Liu et al. (222).
Total luminescence spectroscopy has also been widely used for
various environmental studies during the review period. Lead et al.
reported the 3D excitation-emission matrix (EEM) fluorescence and
electron microscopy characterization of unfractionated and size
fractionated fresh water colloids (223). Nahorniak and Booksh have
published a paper reporting the use of EEM fluorescence for
determination of benzo[k]fluoranthene and benzo[a]pyrene polycyclic aromatic hydrocarbons at part per billion (ppb) concentrations
in aqueous solution (224). In addition to low detection limit, the
technique afforded detection of PAHs in various complex matrixes,
including aqueous motor oil extract and asphalt leachate. In another
study, the use of synchronous-scan fluorescence for selective detection of sodium dodecylbenzene-sulfonate and pyrene in environmental
samples has been reported (225). Application of the SFS technique
for rapid and simultaneous determination of phenol, resorcinol, and
hydroquinone in air samples was also demonstrated by Pistonesi et
al. (226).
SOLID SURFACE LUMINESCENCE
The Hurtubise group continues to be active in the field of solidmatrix luminescence with reports using solid-matrix phosphorescence to characterize DNA adducts (227, 228) and the investigation of several new sugar-glass systems for solid-matrix
luminescence measurements (229). Correa and Escandar investigated the use of nylon as a novel solid matrix for inducing roomtemperature phosphorescence in a report of the first analytical
determination of adsorbed thiabendazole, a widely used fungicide,
by nylon-induced phosphorimetry (230). The same group also
reported the development of a new flow-injection system combined
with solid-surface fluorescence detection for determination of the
same analyte using nylon powder as the solid support (231).
Previously, Garcia-Reyes et al. combined a multicommuted flow
system and solid surface-fluorescence using C-18 as the solid
support in the determination of thiabendazole (232).
Several investigations have used surface-based fluorescence
imaging techniques for the investigation of molecular adsorption
at various solid surfaces. For example, Yeung and co-workers used
total internal reflection (TIR) fluorescence microscopy to examine
the single molecule adsorption of labeled DNA at compositionally
patterned self-assembled monolayers (233) and at glass surfaces
after treatment with various chemical cleaning methods (234).
Hollmann and Czeslik applied TIR fluorescence to study the
adsorption of proteins at a planar poly(acrylic acid) brush as a
function of solution ionic strength (235). Seeger and co-workers
used a supercritical angle fluorescence biosensor to investigate
the conformational reorientation of immunoglobulin G during
nonspecific interaction with surfaces (236) and the adsorption and
desorption behavior of β-lactoglobulin on a hydrophilic glass
surface (237). Thompson and co-workers investigated the size
dependence of protein diffusion near membrane surfaces using
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TIR-FCS and noted that the membrane surfaces slowed the local
diffusion in a size-dependent manner (238).
In related studies, Petrou et al. described a simple glycerin
treatment followed by an incubation period that effectively suppressed fluorescence self-quenching in immunoassays (239). The
treatment dramatically increased the fluorescence signal measured
directly at the solid surface. Another report provided an investigation of the potential of the fluorescence polarization immunoassay
on a solid surface using dry reagent technology (240).
Several reports appeared during this review period which
described solid surface luminescence for the analysis of agricultural and food products. Examples include the use of front-face
fluorescence in the analysis of wine (241), cereal (242), and
honey (243, 244). Karoui and co-workers used the technique
coupled with chemometric tools to characterize soft cheese (245),
monitor ripening of a semihard cheese (246), and assess the
freshness of eggs (247). Sun et al. have developed a method to
screen for tetracycline residues in fish muscles utilizing CCD
camera-based solid-surface fluorescence (248).
LUMINESCENCE IN CHROMATOGRAPHY,
ELECTROPHORESIS, AND FLOW SYSTEMS
The high sensitivity of luminescence makes it an attractive
approach for detection in chemical separations and flow systems.
Jung et al. have presented an isotachophoresis (ITP) method
integrated with microchip-based capillary electrophoresis devices
and have achieved million-fold sample stacking. This high
performance was the result of a single-column ITP configuration
together with electroosmotic flow suppression and high leading
ion concentration (249). When coupled with a confocal fluorescence detection system, a detection limit of 100 aM Alexa Fluor
488 was achieved (250). A multicolor fluorescence detection
system, which uses an acousto-optic tunable filter, has been
constructed for use in an electrophoretic microdevice. The system
enabled detection of PCR-amplified DNA, the discrimination of
multiple amplicons overlapped in time, and the identification of
amplified biowarfare agents (251).
A microfluidic separation system has also been developed for
two-dimensional differential gel electrophoretic separations of
complex cellular protein mixtures to investigate protein expression
in E. coli. Proteins were covalently labeled with Cy2 and Cy3 and
detected simultaneously with a rotary confocal fluorescence
scanner (252). The Soper group has demonstrated detection of
low-abundant DNA point mutations with a microfabricated flowthrough biochip. A polycarbonate (PC) chip has been used to
perform primary polymerase chain reactions (PCR) followed by
an allele-specific ligation detection reaction. A poly(methyl methacrylate) (PMMA) chip has been developed to monitor LDR
products with fluorescence detection using a universal array
platform. This rapid assay required a total analysis time of 50 min
and afforded an order of magnitude reduction in reagents as
compared to benchtop formats (253). The sequence-dependent
separation of ssDNA fragments was achieved with a guanosine
gel in capillary gel electrokinetic chromatography with LIF
detection (254).
The analysis of cells with CE has been reviewed by Ewing
and co-workers (255). CE coupled with luminescence detection
has continued to expand studies of cellular function in the areas
of neuroscience, oncology, enzymology, immunology, and gene
expression. The Zare research group has designed a microfluidic
device to manipulate, lyse, label, separate, and quantify the protein
content of a single cell using single molecule fluorescence
counting (256). Generic labeling of proteins was achieved through
fluorescent-antibody binding. The use of cylindrical optics has
enabled high-efficiency (approximately 60%) counting of molecules
in micrometer-sized channels. Microchip CE with laser-induced
fluorescence detection (µ-chip CE-LIF) was demonstrated for rapid
analysis of individual mitochondrial events in picoliter-volume
samples taken from a bovine liver preparation (257). The Divichi
group has described metabolic cytometry to analyze glycosphingolipid metabolism in single cells using CE with LIF detection.
The ganglioside G(M1) has been tagged with the fluorescent dye
tetramethylrhodamine, taken up by a culture of pituitary tumor
(AtT-20) cells and its metabolites analyzed (258). Flow cytometers
based on poly(dimethylsiloxane) microfluidic devices have been
fabricated, with fluorescence detection accuracy comparable to
that of a commercial flow cytometer and analysis speeds up to
17 000 particles/s. This high-throughput microfluidic device could
be used in inexpensive stand-alone cytometers or as part of
integrated microanalysis systems (259). An interesting development in microfabricated flow cytometers is the use of a thermoreversible gelation polymer (TGP) as a switching valve. The
sol-gel transformation was locally induced by site-directed
infrared laser irradiation. In the absence of fluorescence signal,
the collection channel was plugged by laser-induced gelation.
When a fluorescence signal was detected from the fluorescently
labeled target cells, the waste channel was plugged by laser
irradiation to achieve cell collection. The sorting of fluorescent
microspheres and E. coli cells expressing fluorescent proteins was
demonstrated using this system (260).
A notable application of fluorescence detection in twodimensional CE is the analysis of Barrett’s esophagus tissues.
Rapid and highly reproducible separation has enabled the identification of 18 features from the homogenate profiles as biogenic
amines and amino acids, fluorescently labeled for detection. The
marked differences in concentrations of some features between
squamous biopsies as compared to Barrett’s and fundal biopsies
from a patient with high-grade dysplasia suggested that 2D-CE
may be of value for rapid characterization of endoscopic and
surgical biopsies (261). The approach of 2D-CE coupled with
ultrasensitive fluorescence detection has been used to characterize
the protein and biogenic amine content of single cells from the
RAW 264.7 murine macrophage cell line (262) and the protein
expression from a single-cell mouse embryo (263).
Dual-color fluorescence coincidence has been reported for realtime detection of single native biomolecules and viruses in a
microfluidic channel. With the use of green and red nanoparticles
to simultaneously recognize two binding sites on a single target,
individual molecules of genes, proteins, and intact viruses were
detected and identified in complex mixtures without target
amplification or probe/target separation (264). A novel encoding
method has been devised to generate multifunctional encoded
particles for high-throughput, highly multiplexed analysis of
biomolecules (265). The probes were fabricated by use of
continuous-flow lithography that combined particle synthesis and
encoding and probe incorporation into a single process to generate
particles bearing more than a million unique codes. With the use
of fluorescence detection, DNA oligomers with encoded particle
libraries were scanned rapidly in a flow-through microfluidic
channel. This multiplexing approach could be extended to genetic
analysis, combinatorial library, and clinical analysis. Confocal
correlation spectroscopy has been used for real-time sizing of
nanoparticles in microfluidic channels (266). This approach
allowed measurement of the sizes of both fluorescent and
nonfluorescent particles, including quantum dots, gold colloids,
latex spheres, and fluorescent beads. Sizes were accurately
measured for particles ranging in diameter from 11 to 300 nm, a
size range which has previously been difficult to probe (267).
Luminescence spectroscopy provides a valuable technique for
probing molecular interactions and flow properties in chemical
separations and flow systems. In a recent review, Wirth and Legg
presented a summary of single molecule studies of molecular
adsorption to silica surfaces that is responsible for peak broadening and asymmetry in chromatography, an important problem in
the separation of pharmaceuticals, peptides, and proteins (268).
Using total internal reflection fluorescence microscopy (TIRFM),
the Yeung research group has studied intermolecular interactions
at the water/fused-silica interface, adsorption behavior and conformational dynamics of DNAs, at the single-molecule level. It was
concluded that hydrophobic interactions and hydrogen bonding
were the driving forces of DNA adsorption to fused-silica at pH 5
(269). In a separate experiment, they studied the adsorption
properties of R-phycoerythrin, an autofluorescent protein, on the
fused-silica surface in CE and in single-molecule experiments. The
capacity factor and desorption rate were estimated from the molecular
counting results (270). The Geng laboratory has probed the heterogeneity of a chromatographic interface using ratiometric
confocal fluorescence microscopy. Spectral imaging of Nile Red
revealed that the heterogeneity in environmental polarity between
silica particles is of microscopic origin for band broadening in
chromatography. The adsorption sites were found to be randomly
distributed in the silica particles and smaller in size than the spatial
resolution of confocal imaging (271). The pressure-driven transport of individual DNA molecules in confined fluidic channels has
also been studied by use of fluorescence microscopy. Two distinct
transport regimes were observed. The pressure-driven mobility
of DNA increased with molecular length in channels higher than
a few times the molecular radius of gyration, whereas DNA
mobility was practically independent of molecular length in thin
channels (272). Three-dimensional distribution of fluidic temperature within microchannels was mapped with high resolution
using fluorescence lifetime imaging in an optically sectioning
microscope (273). This technique has allowed optimization of the
chip design for miniaturized processes, such as on-chip PCR, for
which precise temperature control is important. A three-dimensional microfluidic device has been fabricated for eventual use in
studying communication in an in vitro network of nerve cells
(274). Flow profiles have been characterized with computational
fluid dynamics simulations, confocal fluorescence microscopy, and
carbon-fiber amperometry. This microfluidic system and incorporated cell network will ultimately show how networked neurons
adapt, compensate, and recover after being exposed to different
chemical compounds.
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4561
DYNAMIC LUMINESCENCE MEASUREMENTS
The ever-improving temporal and spatial resolution, the
integration of multiple techniques, and progress in single molecule
detection has ensured that luminescence measurements will
continue to offer indispensable opportunities for deepening our
insight into a host of scientific topics. Dynamic luminescence
techniques in particular offer the unique potential for experimentally mapping distributions and fluctuations within heterogeneous
systems, allowing researchers to unravel complex phenomena in
areas ranging from biophysics and biocatalytic reactions to
quantum-confined systems and even green solvent engineering,
as shown by a number of examples selected from throughout this
review period.
Using the lone tryptophan residue as a molecular reporter, the
Zewail group studied the pH-dependence of solvation dynamics,
structural integrity, and local conformational rigidity within the
binding pocket surrounding Trp-214 in human serum albumin with
femtosecond resolution (275). By replacing a native base pair
located near the end of double-stranded DNA by coumarin 102, a
molecular probe whose emission spectrum is sensitive to the local
electric field, the Berg group observed the appearance of a rapid
(∼5 ps) relaxation process assigned to a “fraying” at the end of
the helix (276). Real-time fluorescence measurements were
recently used to monitor function and structural rearrangements
during a dynamic reaction cycle for ribosome-associated trigger
factor, a cotranslational molecular chaperone first encountered
by nascent polypeptides in bacteria (277).
Using fluorescence autocorrelation and cross-correlation spectroscopy with photon counting histogram analysis, Jung and Van
Orden investigated the folding of a dye-quencher labeled hairpin
DNA. Their measurements supported a three-state mechanism
for the DNA hairpin folding reaction that involved a stable
intermediate form of the DNA hairpin (278). Brennan and coworkers have developed a novel two-point “rigid” ionic labeling
approach for modifying polymeric species containing appropriately
spaced amino groups with the fluorescent probe pyranine. With
the use of this new strategy, pyranine-labeled poly(allylamine) and
poly-D-lysine were studied in sodium silicate sol-gels, revealing
a significant restriction of backbone motion in each case (279).
Webb and co-workers used fluorescence correlation spectroscopy (FCS) to investigate the dynamics of equilibrium structural
fluctuations of the model protein apomyoglobin (280). The
conformational fluctuations were detected by quenching of an
N-terminal fluorescent label by contact with various amino acids
and illustrated the complex scope of folding associated structural
dynamics. Mukhopadhyay et al. recently conducted single molecule fluorescence resonance energy transfer (SM-FRET) and FCS
studies to elucidate the collapsed structure, conformational
fluctuations, and early folding intermediates associated with the
prion-determining domain of yeast prion protein Sup35. Their
results revealed a structural ensemble composed of a multitude
of interconverting species rather than a small number of discrete
monomeric conformers, a result likely to play a key role in the
prion conversion process leading to self-perpetuating amyloidogenesis (281). Based largely on SM-FRET experiments probing
the conformational ensemble of the collapsed unfolded state of
the small cold-shock protein CspTm under near-native conditions,
Hoffmann et al. have suggested that collapse in such systems can
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induce secondary structure in an unfolded state without interfering
with long-range distance distributions characteristic of a random
coil, a situation previously thought to exist only in highly expanded
unfolded proteins (282). Eaton and co-workers also applied SMFRET, supported by all-atom molecular dynamics calculations and
Langevin simulations, to obtain quantitative information on the
mean radius of gyration, end-to-end chain distribution, and
dynamics (conformational averaging) of the unfolded states of the
64-residue R/β protein L in comparison to the 66-residue all-β
CspTm (283).
Barbara and colleagues have reported a flow chamber approach which combines rapid nucleocapsid protein (NC)/nucleic
acid mixing with a broad array of fluorescence single molecule
luminescence tools to unravel the heterogeneous kinetics occurring during the course of NC chaperoned irreversible annealing
of a model transactivation response element (TAR) DNA hairpin
sequence to its complementary TAR RNA hairpin to form an
extended duplex. These authors have demonstrated that the TAR
hairpin reactant was predominantly a single hairpin coated by
multiple NCs with a dynamic secondary structure, involving
equilibrium between a “Y” shaped conformation and a closed one
(284).
Xie and co-workers demonstrated the potential of singlemolecule experiments in elucidating the workings of fundamental
biological processes in living cells by probing gene expression in
live cells, one protein molecule at a time (285). The authors found
that protein molecules were produced in bursts, with each burst
originating from a stochastically transcribed single mRNA molecule. The same group also probed transcription factor dynamics
at the single molecule level in a living cell (286).
Since the recent introduction of air- and water-stable room
temperature ionic liquids (RTILs), research into their potential
applications has grown at an ever accelerating rate. RTILs are
currently under exploration in virtually all areas of chemistry, as
“green” solvents for organic and inorganic synthesis; as electrolytes in batteries, fuel cells, and solar cells; as new types of
energetic materials; as stationary phases in chromatography and
in a variety of other analytical applications; and in fundamental
physical chemistry studies. Recent studies by Arzhantsev et al.
combining results from femtosecond Kerr-gated emission spectroscopy with picosecond time-correlated single photon counting
have enabled observation of the complete solvation response
(dynamic Stokes shift) of the solvatochromic probe trans-4dimethylamino-4′-cyanostilbene dissolved in a range of 1-alkyl-3methylimidazolium and n-propyl-n-methylpyrrolidinium RTILs
(287, 288). These results highlight the fact that dielectric
continuum calculations of the sort previously used to predict
solvation dynamics within dipolar liquids are inadequate for
predicting the response within RTILs. In subsequent work,
Maroncelli and co-workers provide evidence for the presence of
dynamic heterogeneity in two representative RTILs, based on the
excitation wavelength dependence of several dynamical solute
processes, including the rotation and solvation of coumarin 153
(C-153), the isomerization of two malononitriles, and intramolecular charge transfer in crystal violet lactone. According to the
authors, the significant variation with excitation wavelength was
consistent with energetically selected subpopulations relaxing at
distinct rates (289). The Sarkar group has also studied the solvent
and rotational relaxation of C-153 in neat 1-butyl-3-methylimidazolium tetrafluoroborate, [bmim][BF4], and has compared results
to the slowed solvation resulting from confinement of the same
RTIL within micelles formed using octaethylene glycol monoalkyl
ethers as surfactants (290). Ito and Richert used time-resolved
phosphorescence to study the RTIL [bmim][PF6] in its fragile
supercooled state near the glass-transition temperature, Tg.
Comparing the solvation dynamics with the rotational motion of
the probe (quinoxaline) and with the dielectric behavior of the
neat fluid, the authors found that the dynamics in the viscous state
were highly dispersive and showed a super-Arrhenius temperature
dependence, as typical for glass-formers (291).
FLUORESCENCE POLARIZATION, MOLECULAR
DYNAMICS, AND RELATED PHENOMENA
The use of fluorescence polarization continues to grow, both
in terms of the breadth of application and the advancement of
fundamental theory. A rather large body of work was first
identified in the initial literature review and was then pared down
to a representative trend of developments in fluorescence polarization and related phenomena. It should be noted that this review
is not intended to be exhaustive but is a sample of developments
over the time period covered by the review. For the purposes of
this review we use the terms polarization and anisotropy
synonymously.
Single molecule spectroscopy continues to be an evolving
area of research, with experiments now reaching high levels
of sophistication. Several papers have been published which
involve development or application of multiparameter fluorescence detection (MFD). The method simultaneously measures
eight fluorescence parameters or dimensions (anisotropy,
lifetime, intensity, time, excitation spectrum, emission spectrum, quantum yield, and distance between fluorophores)
following pulsed excitation and time-correlated single-photon
counting detection. In 2006, the groups of Widengren and Seidel
reported (292) two general strategies for the identification and
analysis of single molecules in dilute solutions. A dye labeling
scheme for oligonucleotides was demonstrated where 16
different compounds were identified in the mixture. Other
applications of the technique were published in 2007 that
included the investigation of dye-exchange dynamics (293), the
investigation of structural and dynamical heterogeneity in DNA
bound rhodamine dye (294), and the implementation of MFD
imaging (295). The technique used MFD in a confocal apparatus that splits the fluorescence emission into its two
polarization components that were then detected by avalanche
photodiodes. Imaging was accomplished by scanning and
storing the MFD for the three physical dimensions. Two
systems involving sepharose beads and microtubule dynamics
in yeast cells were used to demonstrate the ability of the
technique. A study published in 2006 (296) detailed the use of
probability distribution analysis for fluorescence resonance
energy transfer. In 2007, Kalinin et al. reported an extension
of this theory to apply to fluorescence anisotropy in single
molecule experiments (297). The theory allowed prediction of
the shape of anisotropy histograms for a given ensemble
anisotropy and intensity distribution. The approach was wellsuited for detection of biomolecular heterogeneity.
There were several other papers regarding the dynamics of
single molecules using fluorescence anisotropy. Latychevskaia et
al. have reported a single molecule study of polycrystalline
microstructure of n-hexadecane at a temperature of 1.7 K,
revealing a chromophore-two level system in spatially unresolved
molecules (298). Another solid state study was reported (299)
by Forster et al., where fluctuations of single conjugated polymer
molecules were investigated in a polystyrene matrix at room
temperature. The fluctuations in the degree and direction of
polarization were attributed to changes in the contributions of various
exciton states and selective exciton quenching by triplet states. In
more biologically oriented samples, Wirth’s group reported a novel
study of single molecule polarization behavior of a dye-labeled peptide
binding to the human δ-opiod receptor. It was reported that
nonspecific binding could be differentiated from that of specific
binding by analysis of the polarization and that reorientation of only
a few degrees could be distinguished from the shot noise (300). The
Vanden Bout group has published a study that examines the
limitations of single molecule rotational correlation functions and
the characterization of heterogeneity in molecular environments
(301). A particular emphasis was placed on examining the effects
of high numerical aperture on the correlation function and the
statistical errors propagated from finite measurements. Cao et al.
have also published a study detailing the monitoring of live cells
by fluorescence anisotropy imaging (302). The technique was
shown to provide an efficient method for real-time direct monitoring of the digestion of DNA in live cells. Another study that
examines potential artifacts has been published by Fisz, where
the problem of large excitation-detection apertures was studied
in detail (303). It was reported that values for the emission
anisotropy are affected at excitation-detection cone half angles
greater than 15-20°.
DNA analysis represents an active area of research. Deng et
al. have reported a novel geno-typing assay that could detect single
nucleotide polymorphisms (SNPs) (304). The technique was
based on the measurement of fluorescence anisotropy through a
core/shell fluorescent nanoparticle assembly and a ligase reaction.
The assay was completed in two steps, and the discrimination of
a single base mutation in codon 12 of a K-ras oncogene was
demonstrated as a proof-of-principle. Mestas et al. have reported
the development of a new high-throughput screening assay for
the detection of elongation activity in nucleic acid polymerase
enzymes (305). The assay was demonstrated on a microtiter plate
format and was shown to be a potentially efficient method for
screening compounds that may inhibit nucleic acid binding.
The use of fluorescence anisotropy as a tool to examine chiral
recognition continued during this review period. Xu and McCarroll
have reported detailed investigations of the chiral recognition
behavior of 1,1′-binaphthyl-2,2′-diyl hydrogen phosphate (306) and
[1,1′-binaphthalene]-2,2′-diol (307) in the presence of various
cyclodextrins. Valle et al. also reported a comprehensive study
examining chiral separations in molecular micelle systems using
fluorescence anisotropy, as well as capillary electrophoresis and
NMR spectroscopy (308). Analysis of the anisotropy data indicates
different separation mechanisms for the chiral selectors examined.
Kimaru et al. have reported the use of fluorescence anisotropy as
a general method to characterize chiral discrimination under
conditions mimicking those of chromatographic separations (309).
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4563
Several studies were reported on the use of fluorescence
polarization to study protein interactions. Bader et al. have
reported the development of a time-resolved fluorescence anisotropy imaging method to study clustering in proteins (310). The
method was based on fluorescence resonance energy transfer
(FRET) as evidenced by depolarization of the fluorescence
emission in a homo-FRET event. A high-throughput assay was
described by Lokesh et al. for identification of small molecule
inhibitors of the breast cancer gene 1 nuclear protein (311). Li et
al. introduced a method for protein recognition and real-time
quantitative analysis in homogeneous solutions (312). The assay
was shown to be highly selective and have a detection limit of 1
nM in the case of angiogenin protein.
CCD detector to measure chemiluminescence from an optimized
bioluminescence reaction system (326). Rusling and co-workers
have demonstrated the first electrochemiluminescent arrays for
high-throughput in vitro genotoxicity screening (327). The Bard
group continues to make advances in chemiluminescence including an immunoassay of human C-reactive protein using liposomes
containing Ru(bpy)32+ (bpy ) 2,2′-bipyridine) as labels (328).
In other interesting work, Anslyn and co-workers described
the “off-on” glow response of an assay to detect a chemical warfare
stimulant (329). Detection was based on modulation of the
peroxyoxalate chemiluminescence pathway through the use of an
oximate super nucleophile.
CHEMILUMINESCENCE
Chemiluminescence is a powerful analytical tool. This is
because no excitation light is required and most samples have
little or no unwanted background luminescence. However, the
technique is often limited by low quantum efficiency of the
chemiluminescent probe. The Geddes laboratory has made great
advances in this area over the course of this review period. The
interaction of chemiluminescing species with silver island films
was shown to increase the signal intensity (313). The technique
was extended to include low-power microwave heating and applied
to an ultrafast and ultrasensitive clinical assay (314). Multicolored
microwave-triggered metal-enhanced chemiluminescence using
multiple chemiluminescent species emitting at different wavelengths was demonstrated (315). A model assay sensing platform
with the potential to detect and quantify various biomolecules was
demonstrated to detect femtomoles of biotinylated BSA in less
than 2 min (316). The use of continuous aluminum metal
substrates was investigated to further enhance microwave triggered chemiluminescence, and the extent of enhancement was
shown to depend on the surface geometry of the film (317). Spatial
and temporal control of the microwave triggered chemiluminescence was demonstrated and applied to a protein detection
platform (318). After suggesting the possibility, the same group
reported the observation of surface plasmon-coupled chemiluminescence on a thin continuous silver film (319) and observed
various species emitting in different regions of the visible spectrum
on other metals including aluminum and gold as well as silver
(320). Microwave-triggered surface plasmon coupled chemiluminescence was reported as a rapid, high sensitivity technique for
the detection of surface-bound proteins/enzymes and also potentially DNA/RNA (321).
In related work, Ou et al. have investigated the mechanism
responsible for the surface-enhanced chemiluminescence of luminol at nanoscale-corrugated gold and silver films (322). The
enhancement was found to originate from the catalytic properties
induced by the corrugation. Chemiluminescence-based array
imaging was reported as a new optical strategy for the rapid
screening of gold catalysis (323). Lee et al. reported the in vivo
imaging of hydrogen peroxide using chemiluminescent nanoparticles formulated from peroxalate esters and fluorescent dyes
(324). Jie et al. reported a CdS nanocrystal-based electrochemiluminescence biosensor for the detection of low-density lipoprotein
taking advantage of gold nanoparticle amplification (325).
Yeung and co-workers have reported the first real-time imaging
of single bacterium lysis and leakage events by using an intensified
NEAR-INFRARED FLUORESCENCE
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Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
During the last 2 years, advances in NIR fluorescence have
basically been propelled by new chemistry of NIR fluorescing
compounds rather than new instrument development. Fluorescence in vivo imaging still mostly uses animal models although a
clear trend in moving to possible human use is noted. Tanaka et
al. have described a real time approach to ureteral guidance (330).
NIR imaging was used for early detection and prevention of
ureteral injury vital to the health of the patient. Rats and pigs were
injected with CW800-CA dye into the ureter, and the NIR
fluorescence was visualized. A different approach was taken by
Xu et al. (331) through synthesis of a lysine-based trifunctional
chelate that was utilized as a complexing agent for radiometals
used in medical imaging and the near-infrared dye Cy5.5 allowing
for dual modality imaging. Cheng et al. (332) have developed a
NIR fluorescent analogue of the commonly used diagnostic agent
2-deoxy-2-[18F]fluoro-D-glucose for tumor imaging in cell culture
and living mice. Li et al. (333) have described the synthesis of
two NIR fluorescent probes by linking a carbocyanine fluorophore
and glucosamine. The probes were reported to have a high
quantum yield and low cytotoxicity. In vitro NIR optical imaging
indicated strong intracellular NIR fluorescence in breast epithelial
cell lines.
Kalchenko et al. (334) have used a lipophilic dye 1,1′dioctadecyl-3,3,3′,3′-tetramethylindotricarbocyanine iodide (DiR)
for whole-body optical imaging to monitor normal and leukemic
hematopoietic cell homing in vivo. A similar approach was used
by Leevy et al. (335) for bacterial imaging using probes containing
synthetic zinc(II) dipicolylamine (Zn-DPA) coordination complexes
as affinity groups that are able to selectively bind to the surfaces
of bacterial cells and apoptotic animal cells. Yang et al. (336) have
recognized the importance of lipophilicity of NIR dyes in in vivo
imaging. Highly lipophilic NIR dyes do not circulate long in the
bloodstream. The authors reported the synthesis of PEG-coated,
core-cross-linked polymeric micelles (CCPM) derived from an
amine terminated poly(PEG-methacrylate)-b-poly(triethoxysilyl
propylmethacrylate). A Cy-7-like NIR dye was entrapped in the
core. The probe exhibited prolonged blood half-life and enhanced
uptake in a tumor. Ye et al. (337) have used NIR fluorescence to
study the molecular interactions between arginine–glycine–aspartic acid (RGD) peptides and integrins known to mediate many
biological and pathological processes. The authors describe the
synthesis and evaluation of a series of multimeric RGD compounds
constructed on a dicarboxylic acid-containing NIR fluorescent dye
(cypate) for tumor targeting.
An increasing number of applications have used probes other
than conventional NIR dyes. For example, Jeng et al. (338) have
described the optical detection of DNA hybridization on the
surface of solution suspended single-walled carbon nanotubes
(SWNT) for biological applications. Cherukuri et al. (339) have
used chemically pure SWNT that were intravenously administered
to rabbits and monitored by NIR fluorescence observing that the
blood serum concentration decreased exponentially with a halflife of 1.0 ± 0.1 h without adverse effects. Hwang et al. (340) have
outlined single-stranded DNA conjugated SWNT probes that can
be used to locate particular sequences within DNA strands.
Zhu et al. (341) have prepared and structurally characterized
a new expanded porphyrin which was exploited as a highly
sensitive NIR fluorescent chemodosimeter selective for the detection of Hg(II) ions. The total NIR fluorescence decreased upon
addition of Hg(II) due to fluorescence quenching. A selective and
sensitive chemosensor for Cu(II) based on 8-hydroxyquinoline
was described by Mei et al. (342). Kiyose et al. (343) described
a ratiometric fluorescent zinc ion probe in NIR region, based on
tricarbocyanine chromophore. Zhao and Carreira (344) described
novel NIR fluorescent, conformationally restricted aza-dipyrromethene boron difluoride (aza-BODIPY) dyes with intense
absorption, strong fluorescence, and high chemical and photostability. A different family of dyes was investigated by McDonnell
and O’Shea (345) by using amine substituents on the BF2-chelated
tetraarylazadipyrromethene chromophore that generated a triple
absorption and emission responsive sensor. Significant pH sensitivity was observed in both absorption and fluorescence in the
range from pH 5 to 6 M HCl. A NIR fluorescence tricarbochlorocyanine dye (Cy.7.Cl) was synthesized by Tang et al. (346) and
used for NIR spectrofluorimetric determination of hydrogen
peroxide (H2O2) by flow injection analysis (FIA). Hydrogen
peroxide was determined by mixing Cy.7.Cl with horseradish
peroxidase. As Cy.7.Cl was oxidized, the fluorescence intensity
was measured at 800 nm with excitation at 780 nm. In another
study, Sunahara et al. (347) have systematically examined the
mechanism of the solvent polarity dependence of the fluorescence
of the BODIPY fluorophore and the role of photoinduced electron
transfer by varying the substitution of the benzene moieties at
the 8-position to measure micropolarity of biomolecule moieties
and the surface polarity of living cells. Bouteiller et al. (348)
described the preparation and properties of water soluble NIR
fluorophores that can be potential substitutes of the commercially
available Cy 5.5 and Cy 7.0.
Water soluble metallo-phthalocyanines (MPc) were investigated by Verdree et al. (349) by introducing water solubilizing
moieties to minimize aggregation in aqueous environment.
Basheer et al. (350) have investigated dialkylanthracene containing squaraine dyes possessing intense absorption and emission
in the NIR region by synthesizing a novel class of tertiary
arylamine derivatives by addition of squaric acid to the dimethyl
aminoanthracene ring. Unsymmetrical squaraine dyes were also
synthesized by the condensation of 3-[4-(N,N-dialkylamino) anthracene]-4-hydroxy-cyclobutene-1,2-dione with dialkylanilines. Fu
et al. (351) have developed a novel NIR cyanine, 1-(ε-succinimidylhexanoate)-1′-methyl-3,3,3′,3′-tetramethyl-indocarbocyanine-5,5′disulfonate potassium (MeCy5-OSu), and used it for quantification
of polyamines in human erythrocytes by capillary electrophoresis
with diode LIF detection achieving better than 2 nmol L-1 detection
limits. Erythrocyte polyamines can be used as tumor markers;
hence, quantifications of polyamines in human erythrocytes
confirm the quantitative ability of MeCy5-OSu in complex biological samples. Ohnmacht et al. (352) have developed a chromatographic method for measuring free drug fractions based on an
ultrafast immunoextraction/displacement assay with NIR fluorescent labels. Baek et al. (353) took a very different approach to
achieve long wavelength absorption and fluorescence, well above
1000 nm, utilizing inert and photostable encapsulated lanthanide(III) complexes based on dendritic anthracene ligands that
exhibit strong NIR emission bands via efficient energy transfer
from the excited states of the peripheral antenna to Er(III), Yb(III),
and Nd(III) ions.
A full synthetic and optical study of squaraine-derived rotaxanes
was described by Arunkumar et al. (354) to avoid their inherent
reactivity with nucleophiles and tendency to form nonfluorescent
aggregates in water, problems normally associated with this
otherwise highly fluorescent dye. Umezawa et al. (355) reported
a squaraine dye with emission at 751 nm and a quantum yield of
0.56 in cyclohexane that exhibited linear positive solvatochromic
properties near 780 nm. Thomas et al. (356) reported an
environmentally sensitive thiol-reactive squaraine that was sitespecifically coupled to various mutants of glucose/galactose
binding protein containing an engineered cysteine for attachment.
Strekowski et al. (357) have reported a detailed study evaluating
NIR carbocynine dye stability in the presence of molecular oxygen
under dark and light conditions finding that the heterocyclic
structure has a great influence on the stability. All solutions were
more stable when stored in the dark with benz[c,d]indolium dyes
showing outstanding stabilities including under light conditions.
Wang et al. (358) have developed an optical and nuclear dual
labeled imaging agent by synthesizing a NIR dye containing a
cyclic peptide and the nuclear reagent.
LUMINESCENCE TECHNIQUES IN BIOLOGICAL
AND CLINICAL ANALYSIS
Luminescence spectroscopy continues to expand its significant
impact on biological and clinical sciences. With the outstanding
sensitivity of luminescence, methodologies are being developed
for biosensing and bioimaging with ever increasing spatial
resolution and faster time response. As a powerful tool for studying
molecular structure, interactions, and environments, luminescence
has been used in numerous biological applications; only representative works during the period of this review will be discussed
here. An exciting advancement is the emergence of fluorescence
imaging breaking the resolution limit defined by the diffraction
barrier. With stimulated emission depletion (STED) fluorescence
microscopy, the Hell laboratory has reported far-field fluorescence
nanoscopic imaging that achieved a lateral resolution of 29-60
nm in the focal plane, corresponding to a 5- to 8-fold improvement
over the diffraction barrier. The axial resolution was improved
by 3.5-fold (359, 360). The Zhuang group has achieved multicolor
superresolution imaging by using a family of photoswitchable
fluorescent probes in multicolor stochastic optical reconstruction
microscopy. Spatial resolution of 20-30 nm was demonstrated in
multicolor cell imaging (361). The Selvin laboratory monitored
the transport of melanosomes, or melanin-carrying membrane
organelles, and their interactions with molecular motors inside
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4565
melanophore cells with high spatial (approximately 2 nm) and
temporal (approximately 1 ms) localization accuracy (362).
Single molecule fluorescence has been widely applied to
biological systems. In vivo investigations of single molecule
dynamics inside living cells have attracted considerable attention.
To probe transcription factor dynamics, Xie and co-workers
directly monitored the nonspecific binding of a single lac repressor
to a DNA and its diffusion along the DNA in search of the lac
operator. The kinetics of binding and dissociation of the repressor
in response to metabolic signals was measured with single
molecule spectroscopy (363). The assembly of telomerase, a
cellular ribonucleoprotein (RNP) that maintains chromosome
stability by adding telomeric DNA to the termini of linear
chromosomes, was studied by use of single molecule spectroscopy. Direct observation of complex formation in real time
revealed a hierarchical RNP assembly mechanism: interaction with
the telomerase holoenzyme protein p65 induced structural rearrangement of telomerase RNA, which in turn directed the binding
of the telomerase reverse transcriptase to form the functional
ternary complex (364). Single molecule polarization measurements allowed detection of the orientation of a peptide with high
precision and revealed that the receptors do not freely rotationally
diffuse in the bilayer when they are bound by a peptide (365).
Luminescence techniques are also effective for the analysis of
cellular components, cells, and bioaerosols. The membrane raft
hypothesis postulates the existence of lipid bilayer membrane
heterogeneities or domains that are important for cellular function.
Using fluorescence imaging, Baumgart et al. have demonstrated
that giant plasma membrane vesicles formed from the plasma
membranes of cultured mammalian cells could also segregate into
micrometer-scale fluid phase domains, providing an effective
approach to characterization of biological membrane heterogeneities (366). Intravital flow cytometry was introduced to count
rare circulating cancer cells (CTCs) in vivo as they flowed through
the peripheral vasculature. The tumor cells were labeled with a
fluorescent ligand and counted with multiphoton fluorescence
imaging of superficial blood vessels. Studies in mice with
metastatic tumors have provided evidence that CTCs could be
quantitated weeks before metastatic disease was detected by other
means (367). Rosch et al. have monitored and identified bioaerosols by first selecting the biotic particles with fluorescence
imaging. Identification of the particles was accomplished through
analysis of Raman signals of the biotic particles with support vector
machine (368).
A number of reports have outlined the feasibility of diagnosing
cancers and other diseases by use of tissue fluorescence spectroscopy. The Sevick-Muraca group has evaluated the imaging
performance of a near-IR fluorescent dye in human breast cancer
cells in subcutaneous xenograft models. They reported that a NIR
dye provided a significantly reduced background and enhanced
tumor-to-background ratio for high contrast imaging as compared
to dyes excited in the visible (369). The same group also devised
a novel noncontact fluorescence optical tomography scheme with
multiple area illumination patterns. These imaging data were
processed to generate the interior fluorescence distribution in
tissue by implementing the fluorescence tomography algorithm.
This new scheme produced significant improvements over reconstructions by use of only a single measurement (370). The
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Richards-Kortum laboratory detected cervical intraepithelial dysphasia by fitting the tissue fluorescence spectra to a mathematical
model to analyze the concentrations of light scatterers, light
absorbers, and fluorophores in the epithelium and the stroma.
The model provided quantitative information about molecular
changes during the dysplastic transformation (371). Calibration
standards were established for in vivo fluorescence diagnosis to
enable comparison of tissue data collected by multiple devices
and multiple laboratories (372). A synchronous fluorescence
imaging system with a large field of view has been developed for
cancer diagnosis (373). The ratios of tissue tryptophan fluorescence intensity to phosphorescence intensity (374) and bivariate
differential normalized fluorescence (375) have also been demonstrated to provide excellent tissue classification for cancer
diagnosis. A Laguerre deconvolution technique has been reported
for the analysis of time-resolved autofluorescence spectroscopy
data collected from normal and atherosclerotic aortas. This
technique has great potential for the diagnosis of atherosclerotic
plaques, especially for the detection of macrophages infiltration
in atherosclerotic lesions, a key marker of plaque vulnerability
(376). The Feld group has introduced a novel multimodal
spectroscopy method that combines intrinsic fluorescence spectroscopy, diffuse reflectance spectroscopy, and Raman spectroscopy to detect morphological markers of vulnerable atherosclerotic
plaque (377).
An active direction of research is the development of new
probes for biological sensing and imaging. Molecular imaging
probes targeting specific biological molecules in sample matrices
such as cells and tissue were actively pursued. A porphyrin-based
molecular platform has been reported for dual functional fluorescence/magnetic resonance imaging of zinc. The molecular platform had superior physical properties as compared with earliergeneration zinc sensors including emission in the red and nearIR regions and a large Stokes shift of greater than 230 nm. The
fluorescence intensity was observed to increase by more than 10fold upon zinc binding. The manganese derivative switched the
molecule to an MRI sensor. This synthetic strategy can be easily
adapted to constructing other metal sensors (378). Nanoparticles
represent an exciting alternative to conventional probes, offering
the possibility of attaching multiple moieties for targeting and
sensing, improved stability, and often high fluorescence intensity
with low photobleaching. The Tan laboratory has devised multicolor fluorescence resonance energy transfer (FRET) silica
nanoparticles by doping the particles with three fluorescent dyes.
The fluorescence color output of the nanoparticle was tuned by
use of the doping ratios. The nanoparticles could be excited with
a single wavelength, had a large Stokes shift, and were appropriate
for multiplexed analysis of nucleic acids and proteins (379).
Aptamer-conjugated nanoparticles have been constructed to label
prostate cancer cells (380) and leukemia cells (381). The aptamers
were selected by cell-based SELEX strategy and target the
overexpressed membrane antigens. The binding affinity and
synthetic accessibility of the aptamers, in combination with the
photostability of the fluorescent nanoparticles, provided a powerful
and general tool for cell imaging.
REAGENTS AND PROBES
Several new fluorescent reagents and probes were developed
over this review period. Only a small survey of new developments
can be presented in the limited space provided. The Lakowicz
group has published extensively in the area of metal-enhanced
fluorescence (MEF) in recent years. Significant changes in the
photophysical properties of fluorophores in the presence of
metallic nanostructures and nanoparticles have been demonstrated. Two newly developed long chain nitrobenzoxadiazol
derivatives were used to investigate the polarity effect (382) and
fluorophore distance on MEF (383). Single molecule spectroscopy
was used to investigate fluorescence enhancements and lifetime
reduction of Cy5-labeled oligonucleotides near silver island films
(SiFs) (384). In another study, layer-by-layer assembly was used
as a simple, robust, and inexpensive method to control probe
distance from the surface in an investigation of sulforhodamine
B assembled on SiFs (385). In related work, single cell fluorescence imaging was demonstrated using metal plasmon-coupled
probes (386). Fluorescent metal plasmon-coupled probe labeled
cells were 20-fold brighter than the corresponding free labeled
cells. The potential of luminescent metal nanoparticles as molecule
imaging agents was also explored (387).
Several reports of dye-doped silica nanoparticles have
appeared in the literature. Geddes and co-workers have
reported monodispersed core/shell nanoparticles consisting of
silver nanoparticle cores coated with fluorophore doped silica
shells (388). The potential of metal-enhanced fluorescence
“nanoballs” for cellular imaging and solution based sensing was
demonstrated using Rhodamine 800 within the shell. In other
work, Wang and Tan described multicolor FRET silica nanoparticles with potential as barcoding tags for multiplexed
signaling (389). Wu et al. have described a hybrid silica-nanocrystal-organic dye superstructure allowing a postencoding
strategy with the potential to simplify preparation of multicolor
fluorescent spheres (390). Saavedra and co-workers prepared
and characterized poly(lipid)-coated, fluorophore-doped silica
nanoparticles for biolabeling and cellular imaging (391). Tan
and co-workers discussed the applications of silica nanoparticles
doped with either magnetic materials or fluorescent dye
molecules in separating and analyzing biological molecules
(392). The same group also reported the rapid collection and
detection of leukemia cells using a novel two-nanoparticle assay
with aptamers as the molecular recognition element (393).
Magnetic and fluorescent aptamer-modified nanoparticles were
used for target cell extraction and sensitive cell detection,
respectively. Combining two types of nanoparticles improved
the performance of either particle alone. The technique was
extended for the collection and detection of multiple cancer
cells (394).
Multifunctional probes combining the benefits of fluorescent
and magnetic particles in a single probe have been reported. For
example, a new class of dual-function carriers for optical encoding
and magnetic separation based on silica microbeads embedded
with both semiconductor quantum dots and iron oxide nanocrystals were developed by Nie and co-workers (395). In other work,
Gao et al. have synthesized core/shell nanostructures consisting
of a FePt magnetic core and semiconducting chalcogenicle shells
in a sequential one-pot reaction (396). The same group has
reported the rapid detection of bacteria in human blood through
the combination of fluorescent probes and biofunctional magnetic
nanoparticles (397). Multimodal probes for combined fluorescence
and magnetic resonance imaging have also been reported. In one
example, Talanov et al. have synthesized a PAMAM dendrimerbased nanoprobe with Cy5.5 as the fluorescent probe (398).
Complexation with Gd(III) did not affect the quantum yield, and
the dual modality probe was used to visualize the sentinel lymph
nodes in mice by both MRI and fluorescence.
Reagents for fluorescence imaging continue to be developed.
Of particular interest are probes that allow for subdiffraction limit,
or superresolution, far-field fluorescence imaging. Hess et al. have
developed fluorescence photoactivation localization microscopy
(399). The technique exploits the photoactivatable green fluorescent protein activated by a high-frequency (405 nm) laser and then
excited at a lower frequency for imaging by a CCD. Probe
molecules were either reversibly inactivated or irreversibly photobleached to remove them from the field of view. Betzig et al.
have used numerous sparse subsets of photoactivatable fluorescent proteins for intracellular imaging at nanometer resolution
(400). Bates et al. have introduced a family of photoswitchable
fluorescent probes for multicolor superresolution imaging (401).
Preparation of multiple probes with distinct colors allowed
iterative, color-specific activation for multicolor imaging of biological samples with 20-30 nm resolution. Bock et al. have demonstrated two-color far-field fluorescence imaging inside whole cells
with nanoscale resolution by enabling, recording, and disabling
the emission of the reversible switchable fluorescent protein
rsFastLime and the organic fluorophore Cy5 (402). Shroff and
co-workers have used spectrally distinct photoactivatable fluorescent proteins for superresolution imaging of different pairs of
proteins assembled in adhesion complexes (403).
Advances in hybridization probes continue to appear in the
literature. The Turro group reviewed different approaches for
design of fluorescent hybridization probes including molecular
beacons (MBs) and two- and three-dye binary probes for sensitive
and selective DNA and RNA detection (404). Moerner and coworkers have reported the bulk and single molecule characterization of an improved MB using a pair of new dicyanomethylenedihydrofuran (DCDHF) dyes and H-dimer excitonic behavior of
the fluorophores in close proximity (405). The doubled single
molecule emission intensity of target bound self-quenched intramolecular dimer MBs ensured higher signal-to-background
ratio than conventional fluorophore-quencher MBs and offered a
specific means of discriminating between functional MBs and
spurious fluorescence. Yeung and co-workers have presented an
improved method for quantitative clinical screening of surfacehybridized human papilloma virus DNA using single molecule
imaging (406). Single- and double-probe methods were also
described. In other work, Mirkin and co-workers have demonstrated the use of novel oligonucleotide-modified gold nanoparticle
probes hybridized to fluorophore-labeled complements as “nanoflares” for detecting mRNA in living cells (407). Nanoflares were
shown to exhibit high signaling, low background fluorescence,
and sensitivity to changes in the number of RNA transcripts
present in cells. Geddes and co-workers have reported a fast and
sensitive DNA hybridization assays using microwave-accelerated
metal-enhanced fluorescence (408) and investigated the effects
of low-power microwave heating on this new approach (409).
Many lanthanide-based luminescent reagents have been reported during this review period. Examples include the use of
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4567
europium tetracycline as a probe for nucleoside phosphates (410)
and application of lanthanide-binding tags, short peptide sequences
comprising 15-20 naturally occurring amino acids that bind
Tb(III) with high affinity, in the investigation of protein-peptide
interactions (411). Poupart et al. have synthesized and characterized the photophysical properties of a new terpyridine-based
europium(III) chelate for peptide and protein labeling (412).
A large number of derivatization reagents for use in separation
techniques have been developed during the review period.
Examples include an intramolecular charge transfer-based fluorescent reagent that allowed rapid (15 min) staining for SDS-PAGE
(413) and a new fluorescent derivatizing reagent that improved
the HPLC analysis of amino acids which could not be determined
using traditional labeling reagents (414).
Mark Lowry is currently a postdoctoral researcher under the direction
of Professor Isiah M. Warner at Louisiana State University. He received
his B.A. in chemistry from Central College in Pella, IA, in 1998 and his
Ph.D. under the direction of Professor Maxwell Lei Geng at The University
of Iowa in 2005. His research interests include fluorescence instrumentation, fluorescence imaging and image analysis, single molecule imaging/
spectroscopy, fluorescence correlation spectroscopy, time-resolved fluorescence measurements, and the development of new fluorescence reagents
and probes.
Sayo O. Fakayode is an Assistant Professor in the Department of
Chemistry at Winston-Salem State University, Winston-Salem, North
Carolina. He received his B.Sc. degree in chemistry from University of
Ibadan, Nigeria, in 1994 and received his M.Sc. degree in analytical
chemistry from University of Ibadan, in 1997. He was an Assistant Lecture
in the Department of Chemistry, University of Ibadan, Nigeria, from
1998-2000. He obtained his Ph.D. in analytical chemistry from Baylor
University, Waco, Texas, in 2004 under the supervision of Dr. Marianna
A. Busch and Dr. Kenneth W. Busch. He was a postdoctoral researcher
in Dr. Isiah Warner’s research group at Louisiana State University
between 2004-2007. His research interests include chiral analysis,
guest-host inclusion complexation, analytical spectroscopy, fluorescence
detection of molecules of pharmaceutical, clinical, biomedical and
environmental interest, chemometrics and multivariate analysis, and
experimental design for process optimization and process control.
Maxwell L. Geng is an Associate Professor in the Departments of
Chemistry, Nanoscience and Nanotechnology Institute and the Optical
Science and Technology Center at The University of Iowa. He received
his B.S. degree from the University of Science and Technology of China
in 1986 and his Ph.D from Duke University under the direction of
Professor Linda B. McGown in 1994. He then spent 2 years as a
postdoctoral research associate with Professor John C. Wright at the
University of Wisconsin, Madison. His research interests are in the area
of bioanalytical chemistry. Current efforts include spectroscopy imaging
for cancer diagnosis and the investigation of microscopic details in porous
materials.
Gary A. Baker received his B.S. in chemistry from the State University
of New York at Oswego in Oswego, NY, in 1995. He then pursued
graduate studies under the direction of Professor Frank V. Bright at the
University at Buffalo where he received his Ph.D. in analytical chemistry
in 2001. After carrying out postdoctoral research in the laboratory of T.
Mark McCleskey at Los Alamos National Laboratory, he joined the
research staff in the Chemical Sciences Division at Oak Ridge National
Laboratory. His current research interests include green and morphologycontrolled nanomaterials synthesis, smart polymers, ionic liquids, and
all things luminescent.
Lin Wang received her B.S. degree in genetics from Shandong University
in China. She then joined the Department of Chemistry and Biochemistry
at Southern Illinois University at Carbondale in the fall of 2007, where
she is pursuing her Ph.D. in analytical chemistry under the direction of
Professor Matthew E. McCarroll. Her research is focused on developing
new instrumentation and methodology for the identification of protein
target-ligand interactions using dynamic isoelectric focusing and fluorescence anisotropy.
Matthew E. McCarroll is an Associate Professor in the Department of
Chemistry and Biochemistry at Southern Illinois University. He received
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Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
his B.A. and B.S. degrees in chemistry and interdisciplinary studies from
Appalachian State University in 1994. He then pursued graduate studies
at the University of Idaho under the direction of Professor Ray von
Wandruszka, where he received his Ph.D. in 1998. He then spent 2 years
as a postdoctoral associate under the direction of Professor Isiah M.
Warner at Louisiana State University. In 2000, he joined the faculty at
Southern Illinois University as an Assistant Professor and was promoted
to the rank of Associate Professor in 2007. His research interests are
interdisciplinary in practice and span the traditionally defined boundaries
of analytical and physical chemistry. Current projects include studies in
chiral recognition, the development of fluorescence sensors, and instrumentation development for novel methods of screening protein-ligand
interactions.
Gabor Patonay is a Professor of Analytical Chemistry in the Department
of Chemistry at Georgia State University. He received his M.S. (1973)
and Ph.D. (1979) degrees from the Faculty of Chemistry of the Technical
University of Budapest, Hungary. After graduation, he spent a brief period
at the same school mostly developing new analytical instruments and
techniques. In 1982, he joined Professor Isiah M. Warner’s group at Emory
University as a postdoctoral associate. He joined the faculty of Georgia
State University (GSU) in 1987. Dr. Patonay has been active in several
areas of near-infrared (NIR) fluorescence spectroscopy, including development of new optical detection methods. NIR fluorescence has the highest
utility in applications where the interference is significant, i.e., in biological
samples. During the last several years, Dr. Patonay and his research group
have developed new bioanalytical and biomedical applications using NIR
probes and labels. Lately, his research group has been active in developing
new forensic analytical tools for presumptive trace evidence detection using
NIR dyes.
Isiah M. Warner is a Boyd Professor of the LSU System, Philip W. West
Professor of Analytical and Environmental Chemistry in the Department
of Chemistry at Louisiana State University (LSU). He received his B.S.
degree in chemistry from Southern University in Baton Rouge, Louisiana,
in 1968. He worked at Battelle Northwest in Richland, Washington, for
5 years before pursuing his Ph.D. in Analytical Chemistry from the
University of Washington in 1973. He received his Ph.D. in Analytical
Chemistry from the University of Washington in 1977. He served on the
faculty of Texas A&M University for 5 years and on the faculty of Emory
University for 10 years before joining the faculty of LSU in 1992. His
research interests include fluorescence spectroscopy, studies in organized
media, and separation science, with a focus on solving biomedical and
environmental analytical problems.
LITERATURE CITED
(1) Fletcher, K. A.; Fakayode, S. O.; Lowry, M.; Tucker, S. A.; Neal, S. L.;
Kimaru, I. W.; McCarroll, M. E.; Patonay, G.; Oldham, P. B.; Rusin, O.;
Strongin, R. M.; Warner, I. M. Anal. Chem. 2006, 78, 4047–4068.
BOOKS, REVIEWS, AND CHAPTERS OF
GENERAL INTEREST
(2) Lakowicz, J. R. Principles of Fluorescence Spectroscopy, 3rd ed.; Springer:
New York, 2006.
(3) Reviews in Fluorescence 2006; Geddes, C. D., Lakowicz, J. R., Eds.;
Springer: New York, 2006; Vol. 3.
(4) Who’s Who in Fluorescence 2006; Geddes, C. D., Lakowicz, J. R., Eds.;
Springer: New York, 2006.
(5) Who’s Who in Fluorescence 2007; Geddes, C. D., Lakowicz, J. R., Eds.;
Springer: New York, 2006.
(6) Fluorescence of Supermolecules, Polymers, and Nanosystems; BerberanSantos, M. N., Ed.; Springer: New York, 2007.
(7) Glucose Sensing (Topics in Fluorescence Sprectroscopy); Geddes, C. D.,
Lakowicz, J. R., Eds.; Springer: New York, 2006.
(8) Fluorescent Energy Transfer Nucleic Acid Probes: Designs and Protocols;
Didenko, V. V., Ed.; Methods in Molecular Biology; Humana Press:
Totowa, NJ, 2006.
(9) Gell, C.; Brockwell, D.; Smith, A. Handbook of Single Molecule Fluorescence
Spectroscopy; Oxford University Press: New York, 2006.
(10) Moerner, W. E. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 12596–12602.
(11) Giepmans, B. N. G.; Adams, S. R.; Ellisman, M. H.; Tsien, R. Y. Science
2006, 312, 217–224.
(12) Michalet, X.; Weiss, S.; Jager, M. Chem. Rev 2006, 106, 1785–1813.
(13) Sapsford, K. E.; Berti, L.; Medintz, I. L. Angew. Chem., Int. Ed. 2006, 45,
4562–4588.
(14) Basabe-Desmonts, L.; Reinhoudt, D. N.; Crego-Calama, M. Chem. Soc. Rev.
2007, 36, 993–1017.
(15) Costa-Fernandez, J. M.; Pereiro, R.; Sanz-Medel, A. TrAC, Trends Anal.
Chem. 2006, 25, 207–218.
(16) Burns, A.; Ow, H.; Wiesner, U. Chem. Soc. Rev. 2006, 35, 1028–1042.
(17) Su, Y. Y.; Chen, H.; Wang, Z. M.; Lv, Y. Appl. Spectrosc. Rev. 2007, 42,
139–176.
(18) Diaz-Garcia, M. E.; Fernandez-Gonzalez, A.; Badia-Laino, R. Appl. Spectrosc.
Rev. 2007, 42, 605–624.
GENERAL INSTRUMENTATION
(19) Valledor, M.; Carlos Campo, J.; Sanchez-Barragan, I.; Carlos Viera, J.;
Costa-Fernandez, J. M.; Sanz-Medel, A. Sens. Actuators, B: Chem. 2006,
117, 266–273.
(20) Bromage, E. S.; Lackie, T.; Unger, M. A.; Ye, J.; Kaattari, S. L. Biosens.
Bioelectron. 2007, 22, 2532–2538.
(21) Lu, J. J.; Pu, Q. S.; Wang, S. L.; Liu, S. R. Anal. Chim. Acta 2007, 590,
98–103.
(22) Casado-Terrones, S.; Cortacero-Ramirez, S.; Carrasco-Pancorbo, A.; SeguraCarretero, A.; Fernandez-Gutierrez, A. Anal. Bioanal. Chem 2006, 386,
1835–1847.
(23) Cottrell, W. J.; Oseroff, A. R.; Foster, T. H. Rev. Sci. Instrum. 2006, 77,
064302.
(24) Jayachandran, B.; Ge, J. J.; Regalado, S.; Godavarty, A. J. Biomed. Opt.
2007, 12, 054014.
(25) Liu, P.; Seo, T. S.; Beyor, N.; Shin, K. J.; Scherer, J. R.; Mathies, R. A.
Anal. Chem. 2007, 79, 1881–1889.
(26) Marwani, H. M.; Lowry, M.; Keating, P.; Warner, I. M.; Cook, R. L. J.
Fluoresc. 2007, 17, 687–699.
(27) Dumke, J. C.; Nussbaum, M. A. Anal. Chem. 2007, 79, 1262–1265.
(28) Kraikivski, P.; Pouligny, B.; Dimova, R. Rev. Sci. Instrum. 2006, 77,
113703.
(29) Gilmore, A.; Cohen, S. M.; Sagoo, K. Am. Lab. 2007, 39, 15–17.
(30) Kannan, B.; Har, J. Y.; Liu, P.; Maruyama, I.; Ding, J. L.; Wohland, T.
Anal. Chem. 2006, 78, 3444–3451.
(31) Rech, I.; Cova, S.; Restelli, A.; Ghioni, M.; Chiari, M.; Cretich, M.
Electrophoresis 2006, 27, 3797–3804.
(32) Michalet, X.; Siegmund, O. H. W.; Vallerga, J. V.; Jelinsky, P.; Millaud,
J. E.; Weiss, S. J. Mod. Opt. 2007, 54, 239–281.
(33) Finkelstein, H.; Hsu, M. J.; Zlatanovic, S.; Esener, S. Rev. Sci. Instrum.
2007, 78, 103103.
(34) Zeng, S. Q.; Lv, X.; Zhan, C.; Chen, W. R.; Xiong, W. H.; Jacques, S. L.;
Luo, Q. M. Opt. Lett. 2006, 31, 1091–1093.
(35) Wolleschensky, R.; Zimmermann, B.; Kempe, M. J. Biomed. Opt. 2006,
11, 05371RR.
(36) Ren, K. N.; Liang, Q. L.; Yao, B.; Luo, G. O.; Wang, L. D.; Gao, Y.; Wang,
Y. M.; Qiu, Y. Lab Chip 2007, 7, 1574–1580.
(37) Poher, V.; Zhang, H. X.; Kennedy, G. T.; Griffin, C.; Oddos, S.; Gu, E.;
Elson, D. S.; Girkin, J. M.; French, P. M. W.; Dawson, M. D.; Neil, M. A. A.
Opt. Express 2007, 15, 11196–11206.
(38) Moser, C.; Mayr, T.; Klimant, I. J. Microsc. (Oxford, U.K.) 2006, 222,
135–140.
(39) McGuinness, C. D.; Macmillan, A. M.; Sagoo, K.; McLoskey, D.; Birch,
D. J. S. Appl. Phys. Lett. 2006, 89, 063901.
(40) de Jong, E. P.; Lucy, C. A. Analyst 2006, 131, 664–669.
(41) Pfeifer, D.; Hoffmann, K.; Hoffmann, A.; Monte, C.; Resch-Genger, U. J.
Fluoresc. 2006, 16, 581–587.
(42) DeRose, P. C.; Early, E. A.; Kramer, G. W. Rev. Sci. Instrum. 2007, 78,
033107.
(43) Boens, N.; Qin, W. W.; Basaric, N.; Hofkens, J.; Ameloot, M.; Pouget, J.;
Lefevre, J. P.; Valeur, B.; Gratton, E.; Vandeven, M.; Silva, N. D.;
Engelborghs, Y.; Willaert, K.; Sillen, A.; Rumbles, G.; Phillips, D.; Visser,
A. J. W. G.; van Hoek, A.; Lakowicz, J. R.; Malak, H.; Gryczynski, I.; Szabo,
A. G.; Krajcarski, D. T.; Tamai, N.; Miura, A. Anal. Chem. 2007, 79, 2137–
2149.
(44) Elder, A. D.; Frank, J. H.; Swartling, J.; Dai, X.; Kaminski, C. F. J. Microsc.
(Oxford, U.K.) 2006, 224, 166–180.
(45) Cho, E. H.; Lockett, S. J. J. Microsc. (Oxford, U.K.) 2006, 223, 15–25.
(46) Gao, Y.; Zhong, Z. M.; Geng, M. L. Appl. Spectrosc. 2007, 61, 956–962.
(47) Pelet, S.; Previte, M. J. R.; So, P. T. C. J. Biomed. Opt. 2006, 11, 034017.
(48) Domingo, B.; Sabariegos, R.; Picazo, F.; Llopis, J. Microsc. Res. Tech. 2007,
70, 1010–1021.
(49) Marin, N. M.; MacKinnon, N.; MacAulay, C.; Chang, S. K.; Atkinson, E. N.;
Cox, D.; Serachitopol, D.; Pikkula, B.; Follen, M.; Richards-Kortum, R.
J. Biomed. Opt. 2006, 11, 014010.
(50) Pikkula, B. M.; Shuhatovich, O.; Price, R. L.; Serachitopol, D. M.; Follen,
M.; McKinnon, N.; MacAulay, C.; Richards-Kortum, R.; Lee, J. S.; Atkinson,
E. N. J. Biomed. Opt. 2007, 12, 034014.
LASER-BASED TECHNIQUES
(51) Smith, B. TrAC, Trends Anal. Chem. 2007, 26, 60–64.
(52) Ray, A. K.; Sinha, S.; Kundu, S.; Kumar, S.; Dasgupta, K. Appl. Phys. B:
Lasers Opt. 2007, 87, 489–495.
(53) Garcia-Moreno, I.; Amat-Guerri, F.; Liras, M.; Costela, A.; Infantes, L.;
Sastre, R.; Arbeloa, F. L.; Prieto, J. B.; Arbeloa, I. L. Adv. Funct. Mater.
2007, 17, 3088–3098.
(54) Kano, H.; Hamaguchi, H. Opt. Express 2006, 14, 2798–2804.
(55) Frank, J. H.; Elder, A. D.; Swartling, J.; Venkitaraman, A. R.; Jeyasekharan,
A. D.; Kaminski, C. F. J. Microsc. (Oxford, U.K.) 2007, 227, 203–215.
(56) Li, Q.; Seeger, S. Anal. Chem. 2006, 78, 2732–2737.
(57) Pappas, D.; Burrows, S. M.; Reif, R. D. TrAC, Trends Anal. Chem. 2007,
26, 884–894.
(58) Seelig, J.; Leslie, K.; Renn, A.; Kuhn, S.; Jacobsen, V.; van de Corput, M.;
Wyman, C.; Sandoghdar, V. Nano Lett. 2007, 7, 685–689.
(59) Lee, N. K.; Kapanidis, A. N.; Koh, H. R.; Korlann, Y.; Ho, S. O.; Kim, Y.;
Gassman, N.; Kim, S. K.; Weiss, S. Biophys. J. 2007, 92, 303–312.
(60) Widengren, J.; Chmyrov, A.; Eggeling, C.; Lofdahl, P. A.; Seidel, C. A. M.
J. Phys. Chem. A 2007, 111, 429–440.
(61) Ito, S.; Sugiyama, T.; Toitani, N.; Katayama, G.; Miyasaka, H. J. Phys. Chem.
B 2007, 111, 2365–2371.
(62) Li, H. T.; Zhou, D. J.; Browne, H.; Klenerman, D. J. Am. Chem. Soc. 2006,
128, 5711–5717.
(63) Merenda, F.; Rohner, J.; Fournier, J. M.; Salathe, R. P. Opt. Express 2007,
15, 6075–6086.
(64) Leutenegger, M.; Gosch, M.; Perentes, A.; Hoffmann, P.; Martin, O. J. F.;
Lasser, T. Opt. Express 2006, 14, 956–969.
(65) Borejdo, J.; Calander, N.; Gryczynski, Z.; Gryczynski, I. Opt. Express 2006,
14, 7878–7888.
(66) Garai, K.; Muralidhar, M.; Maiti, S. Appl. Opt. 2006, 45, 7538–7542.
(67) Sonehara, T.; Anazawa, T.; Uchida, K. Anal. Chem. 2006, 78, 8395–8405.
(68) Hwang, L. C.; Leutenegger, M.; Gosch, M.; Lasser, T.; Rigler, P.; Meier,
W.; Wohland, T. Opt. Lett. 2006, 31, 1310–1312.
(69) Culbertson, M. J.; Burden, D. L. Rev. Sci. Instrum. 2007, 78, 044102.
(70) Mutze, J.; Petrasek, Z.; Schwille, P. J. Fluoresc. 2007, 17, 805–810.
(71) Kolin, D. L.; Costantino, S.; Wiseman, P. W. Biophys. J. 2006, 90, 628–
639.
(72) Rothstein, E. C.; Nauman, M.; Chesnick, S.; Balaban, R. S. J. Microsc.
(Oxford, U.K.) 2006, 222, 58–64.
(73) Joo, C.; Kim, K. H.; de Boer, J. F. Opt. Lett. 2007, 32, 623–625.
(74) Liu, L.; Qu, J.; Lin, Z.; Wang, L.; Fu, Z.; Guo, B.; Niu, H. Appl. Phys. B:
Lasers Opt. 2006, 84, 379–383.
(75) Bird, D. K.; Eliceiri, K. W.; White, J. G. J. Microsc. (Oxford, U.K.) 2006,
224, 249–255.
(76) Ragan, T.; Huang, H. D.; So, P.; Gratton, E. J. Fluoresc. 2006, 16, 325–
336.
(77) McConnell, G. J. Biomed. Opt. 2006, 11, 054020.
(78) Bahlmann, K.; So, P. T. C.; Kirber, M.; Reich, R.; Kosicki, B.; McGonagle,
W.; Bellve, K. Opt. Express 2007, 15, 10991–10998.
(79) Amir, W.; Carriles, R.; Hoover, E. E.; Planchon, T. A.; Durfee, C. G.; Squier,
J. A. Opt. Lett. 2007, 32, 1731–1733.
(80) Haeberle, O.; Simon, B. Opt. Commun. 2006, 259, 400–408.
(81) Rice, J. H. Mol. Biosyst. 2007, 3, 781–793.
(82) Hell, S. W. Science 2007, 316, 1153–1158.
SENSORS
(83) Viveros, L.; Paliwal, S.; McCrae, D.; Wild, J.; Simonian, A. Sens. Actuators,
B: Chem. 2006, 115, 150–157.
(84) Ramanathan, M.; Simonian, A. L. Biosens. Bioelectron. 2007, 22, 3001–
3007.
(85) Knapton, D.; Burnworth, M.; Rowan, S. J.; Weder, C. Angew. Chem., Int.
Ed. 2006, 45, 5825–5829.
(86) Dale, T. J.; Rebek, J. J. Am. Chem. Soc. 2006, 128, 4500–4501.
(87) Wallace, K. J.; Fagbemi, R. I.; Folmer-Andersen, F. J.; Morey, J.; Lynth,
V. M.; Anslyn, E. V. Chem. Commun. 2006, 3886–3888.
(88) Nguyen, B. T.; Anslyn, E. V. Coord. Chem. Rev. 2006, 250, 3118–3127.
(89) Schiller, A.; Wessling, R. A.; Singaram, B. Angew. Chem., Int. Ed. 2007,
46, 6457–6459.
(90) Cordes, D. B.; Gamsey, S.; Singaram, B. Angew. Chem., Int. Ed. 2006,
45, 3829–3832.
(91) Cordes, D. B.; Miller, A.; Gamsey, S.; Singaram, B. Anal. Bioanal. Chem.
2007, 387, 2767–2773.
(92) Jiang, S.; Escobedo, J. O.; Kim, K. K.; Alpturk, O.; Samoei, G. K.; Fakayode,
S. O.; Warner, I. M.; Rusin, O.; Strongin, R. M. J. Am. Chem. Soc. 2006,
128, 12221–12228.
(93) Alpturk, O.; Rusin, O.; Fakayode, S. O.; Wang, W. H.; Escobedo, J. O.;
Warner, I. M.; Crowe, W. E.; Kral, V.; Pruet, J. M.; Strongin, R. M. Proc.
Natl. Acad. Sci. U.S.A. 2006, 103, 9756–9760.
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4569
(94) Chen, H. L.; Zhao, Q.; Wu, Y. B.; Li, F. Y.; Yang, H.; Yi, T.; Huang, C. H.
Inorg. Chem. 2007, 46, 11075–11081.
(95) Zhang, M.; Li, M. Y.; Zhao, Q.; Li, F. Y.; Zhang, D. Q.; Zhang, J. P.; Yi, T.;
Huang, C. H. Tetrahedron Lett. 2007, 48, 2329–2333.
(96) Zhang, M.; Yu, M. X.; Li, F. Y.; Zhu, M. W.; Li, M. Y.; Gao, Y. H.; Li, L.;
Liu, Z. Q.; Zhang, J. P.; Zhang, D. Q.; Yi, T.; Huang, C. H. J. Am. Chem.
Soc. 2007, 129, 10322–10323.
(97) Zguris, J.; Pishko, M. V. Sens. Actuators, B: Chem. 2006, 115, 503–509.
(98) Kim, W. S.; Ye, X. Y.; Rubakhin, S. S.; Sweedler, J. V. Anal. Chem. 2006,
78, 1859–1865.
(99) Lim, M. H.; Lippard, S. J. Acc. Chem. Res. 2007, 40, 41–51.
(100) Schroder, C. R.; Polerecky, L.; Klimant, I. Anal. Chem. 2007, 79, 60–70.
(101) Kocincova, A. S.; Borisov, S. M.; Krause, C.; Wolfbeis, O. S. Anal. Chem.
2007, 79, 8486–8493.
(102) Charier, S.; Ruel, O.; Baudin, J. B.; Alcor, D.; Allemand, J. F.; Meglio, A.;
Jullien, L.; Valeur, B. Chem.sEur. J. 2006, 12, 1097–1113.
(103) Holthoff, E. L.; Bright, F. V. Anal. Chim. Acta 2007, 594, 147–161.
(104) Tao, Z. Y.; Tehan, E. C.; Bukowski, R. M.; Tang, Y.; Shughart, E. L.;
Holthoff, W. G.; Cartwright, A. N.; Titus, A. H.; Bright, F. V. Anal. Chim.
Acta 2006, 564, 59–65.
(105) Thomas, S. W.; Joly, G. D.; Swager, T. M. Chem. Rev. 2007, 107, 1339–
1386.
(106) Li, J.; Kenclig, C. E.; Nesterov, E. E. J. Am. Chem. Soc. 2007, 129, 15911–
15918.
(107) Fan, L. J.; Jones, W. E. J. Am. Chem. Soc. 2006, 128, 6784–6785.
(108) van Dongen, E.; Evers, T. H.; Dekkers, L. M.; Meijer, E. W.; Klomp,
L. W. J.; Merkx, M. J. Am. Chem. Soc. 2007, 129, 3494–3495.
(109) Komatsu, K.; Urano, Y.; Kojima, H.; Nagano, T. J. Am. Chem. Soc. 2007,
129, 13447–13454.
(110) Zeng, L.; Miller, E. W.; Pralle, A.; Isacoff, E. Y.; Chang, C. J. J. Am. Chem.
Soc. 2006, 128, 10–11.
(111) Yang, H.; Liu, Z. Q.; Zhou, Z. G.; Shi, E. X.; Li, F. Y.; Du, Y. K.; Yi, T.;
Huang, C. H. Tetrahedron Lett. 2006, 47, 2911–2914.
(112) Nolan, E. M.; Lippard, S. J. J. Am. Chem. Soc. 2007, 129, 5910–5918.
(113) Zhao, Y. P.; Zhao, C. C.; Wu, L. Z.; Zhang, L. P.; Tung, C. H.; Pan, Y. J. J.
Org. Chem. 2006, 71, 2143–2146.
(114) Zyryanov, G. V.; Palacios, M. A.; Anzenbacher, P. Angew. Chem., Int. Ed.
2007, 46, 7849–7852.
(115) Gunnlaugsson, T.; Glynn, M.; Tocci, G. M.; Kruger, P. E.; Pfeffer, F. M.
Coord. Chem. Rev. 2006, 250, 3094–3117.
SAMPLE PREPARATION, QUENCHING, AND
RELATED PHENOMENA
(116) Cognet, L.; Tsyboulski, D. A.; Rocha, J. D. R.; Doyle, C. D.; Tour, J. M.;
Weisman, R. B. Science 2007, 316, 1465–1468.
(117) Schneider, G.; Decher, G.; Nerambourg, N.; Praho, R.; Werts, M. H. V.;
Blanchard-Desce, M. Nano Lett. 2006, 6, 530–536.
(118) Jennings, T. L.; Singh, M. P.; Strouse, G. F. J. Am. Chem. Soc. 2006,
128, 5462–5467.
(119) Pons, T.; Medintz, I. L.; Sapsford, K. E.; Higashiya, S.; Grimes, A. F.;
English, D. S.; Mattoussi, H. Nano Lett. 2007, 7, 3157–3164.
(120) Laferriere, M.; Galian, R. E.; Maurel, V.; Scaiano, J. C. Chem. Commun.
2006, 257–259.
(121) Huang, H.; Dorn, A.; Nair, G. P.; Bulovic, V.; Bawendi, M. G. Nano Lett.
2007, 7, 3781–3786.
(122) Wu, H. P.; Cheng, T. L.; Tseng, W. L. Langmuir 2007, 23, 7880–7885.
(123) Kumar, S.; Singh, P.; Kaur, S. Tetrahedron 2007, 63, 11724–11732.
(124) Wang, X.; Zeng, H. L.; Zhao, L. X.; Lin, J. M. Talanta 2006, 70, 160–168.
(125) Wu, C. Y.; Chen, M. S.; Lin, C. A.; Lin, S. C.; Sun, S. S. Chem.sEur. J.
2006, 12, 2263–2269.
(126) He, F.; Tang, Y. L.; Yu, M. H.; Wang, S.; Li, Y. H.; Zhu, D. B. Adv. Funct.
Mater. 2007, 17, 996–1002.
(127) Muller, J. G.; Atas, E.; Tan, C.; Schanze, K. S.; Kleiman, V. D. J. Am. Chem.
Soc. 2006, 128, 4007–4016.
(128) Liao, J. H.; Swager, T. M. Langmuir 2007, 23, 112–115.
(129) Ramanavicius, A.; Kurilcik, N.; Jursenas, S.; Finkelsteirtas, A.; Ramanaviciene, A. Biosens. Bioelectron. 2007, 23, 499–505.
(130) Ao, L. M.; Gao, F.; Pan, B. F.; He, R.; Cui, D. X. Anal. Chem. 2006, 78,
1104–1106.
(131) Baker, S. N.; Brauns, E. B.; McCleskey, T. M.; Burrell, A. K.; Baker, G. A.
Chem. Commun. 2006, 2851–2853.
(132) Abe, H.; Kool, E. T. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 263–268.
(133) Rupcich, N.; Chiuman, W.; Nutiu, R.; Mei, S.; Flora, K. K.; Li, Y. F.;
Brennan, J. D. J. Am. Chem. Soc. 2006, 128, 780–790.
(134) Bulygin, V. V.; Milgrom, Y. M. Proc. Natl. Acad. Sci. U.S.A. 2007, 104,
4327–4331.
4570
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
DATA REDUCTION
(135) Yang, L. J.; Li, Y. B. Analyst 2006, 131, 394–401.
(136) Griffiths, M. L.; Barbagallo, R. P.; Keer, J. T. Anal. Chem. 2006, 78, 513–
523.
(137) Tran, C. D.; Oliveira, D. Anal. Biochem. 2006, 356, 51–58.
(138) Fakayode, S. O.; Williams, A. A.; Busch, M. A.; Busch, K. W.; Warner,
I. M. J. Fluoresc. 2006, 16, 659–670.
(139) Niazi, A.; Sadeghi, M. Chem. Pharm. Bull. 2006, 54, 711–713.
(140) Pulgarin, J. A. M.; Bermejo, L. F. G.; Garcia, M. N. S. Anal. Chim. Acta
2007, 602, 66–74.
(141) Piccirilli, G. N.; Escandar, G. M. Analyst 2006, 131, 1012–1020.
(142) Gil, D. B.; de la Pena, A. M.; Arancibia, J. A.; Escandar, G. M.; Olivieri,
A. C. Anal. Chem. 2006, 78, 8051–8058.
(143) Damiani, P. C.; Duran-Meras, I.; Garcia-Reiriz, A.; Jimenez-Giron, A.; de
la Pena, A. M.; Olivieri, A. C. Anal. Chem. 2007, 79, 6949–6958.
(144) Escandar, G. M.; Faber, N. K. M.; Goicoechea, H. C.; de la Pena, A. M.;
Olivieri, A. C.; Poppi, R. J. TrAC, Trends Anal. Chem. 2007, 26, 752–765.
(145) Aghamohammadi, M.; Hashemi, J.; Kram, G. A.; Alizadeh, N. Anal. Chim.
Acta 2007, 582, 288–294.
(146) Fisz, J. J. J. Phys. Chem. A 2006, 110, 12977–12985.
(147) Di Nezio, M. S.; Pistonesi, M. F.; Fragoso, W. D.; Pontes, M. J. C.;
Goicoechea, H. C.; Araujo, M. C. U.; Band, B. S. F. Microchem. J. 2007,
85, 194–200.
(148) Bosco, M. V.; Garrido, M.; Larrechi, M. S. Anal. Chim. Acta 2006, 559,
240–247.
(149) Bosco, M. V.; Callao, M. P.; Larrechi, M. S. Anal. Chim. Acta 2006, 576,
184–191.
(150) Banaitis, M. R.; Waldrip-Dail, H.; Diehl, M. S.; Holmes, B. C.; Hunt, J. F.;
Lynch, R. P.; Ohno, T. J. Colloid Interface Sci. 2006, 304, 271–276.
(151) Hunt, J. F.; Ohno, T. J. Agric. Food Chem. 2007, 55, 2121–2128.
(152) Zhang, F.; Zhang, Q. Q.; Wang, W. G.; Wang, X. L. J. Photochem. Photobiol.,
A 2006, 184, 241–249.
(153) Surribas, A.; Amigo, J. M.; Coello, J.; Montesinos, J. L.; Valero, F.; Maspoch,
S. Anal. Bioanal. Chem. 2006, 385, 1281–1288.
(154) Zhou, H. C.; Baldini, L.; Hong, J.; Wilson, A. J.; Hamilton, A. D. J. Am.
Chem. Soc. 2006, 128, 2421–2425.
(155) Kunnil, J.; Sarasanandarajah, S.; Chacko, E.; Reinisch, L. Appl. Opt. 2006,
45, 3659–3664.
(156) Karoui, R.; Dufour, E.; De Baerdemaeker, J. Food Chem. 2007, 101, 1305–
1314.
(157) Rowe, B. A.; Neal, S. L. J. Phys. Chem. B 2006, 110, 15021–15028.
(158) Kamath, S. D.; Mahato, K. K. J. Biomed. Opt. 2007, 12, 014028.
(159) Whitaker, R. D.; Walt, D. R. Anal. Chem. 2007, 79, 9045–9053.
(160) Arancibia, J. A.; Escandar, G. M. Anal. Chim. Acta 2007, 584, 287–294.
(161) Garcia-Reiriz, A.; Damiani, P. C.; Olivieri, A. C. Anal. Chim. Acta 2007,
588, 192–199.
(162) Miranda, O. R.; You, C. C.; Phillips, R.; Kim, I. B.; Ghosh, P. S.; Bunz,
U. H. F.; Rotello, V. M. J. Am. Chem. Soc. 2007, 129, 9856–9857.
(163) Hall, G. J.; Kenny, J. E. Anal. Chim. Acta 2007, 581, 118–124.
(164) Norgaard, L.; Soletormos, G.; Harrit, N.; Albrechtsen, M.; Olsen, O.;
Nielsen, D.; Kampmann, K.; Bro, R. J. Chemom. 2007, 21, 451–458.
(165) Malachowski, G. C.; Clegg, R. M.; Redford, G. I. J. Microsc. (Oxford, U.K.)
2007, 228, 282–295.
(166) Kudryavtsev, V.; Felekyan, S.; Wozniak, A. K.; Konig, M.; Sandhagen, C.;
Kuhnemuth, R.; Seidel, C. A. M.; Oesterhelt, F. Anal. Bioanal. Chem.
2007, 387, 71–82.
(167) Widengren, J.; Kudryavtsev, V.; Antonik, M.; Berger, S.; Gerken, M.; Seidel,
C. A. M. Anal. Chem. 2006, 78, 2039–2050.
(168) Jung, J. Y.; Van Orden, A. J. Am. Chem. Soc. 2006, 128, 1240–1249.
(169) Werner, J. H.; Joggerst, R.; Dyer, R. B.; Goodwin, P. M. Proc. Natl. Acad.
Sci. U.S.A. 2006, 103, 11130–11135.
(170) Burkhardt, M.; Schwille, P. Opt. Express 2006, 14, 5013–5020.
(171) Culbertson, M. J.; Williams, J. T. B.; Cheng, W. W. L.; Stults, D. A.;
Wiebracht, E. R.; Kasianowicz, J. J.; Burden, D. L. Anal. Chem. 2007,
79, 4031–4039.
ORGANIZED MEDIA
(172) Rodriguez, J. J. S.; Halko, R.; Rodriguez, J. R. B.; Aaron, J. J. Anal. Bioanal.
Chem. 2006, 385, 525–545.
(173) Fakayode, S. O.; Lowry, M.; Fletcher, K. A.; Huang, X. D.; Powe, A. M.;
Warner, I. M. Curr. Anal. Chem. 2007, 3, 171–181.
(174) Mohanty, J.; Bhasikuttan, A. C.; Nau, W. M.; Pal, H. J. Phys. Chem. B 2006,
110, 5132–5138.
(175) Liu, Y.; Li, C. J.; Guo, D. S.; Pan, Z. H.; Li, Z. Supramol. Chem. 2007, 19,
517–523.
(176) Sun, J.; Zhu, X. S.; Wu, M. J. Fluoresc. 2007, 17, 265–270.
(177) Canada-Canada, F.; Rodriguez-Caceres, M. I. J. Fluoresc. 2007, 17, 23–
28.
(178) Zhang, X. H.; Wang, Y.; Jin, W. J. Talanta 2007, 73, 938–942.
(179) Fakayode, S. O.; Williams, A. A.; Busch, M. A.; Busch, K. W.; Warner,
I. M. J. Fluoresc. 2006, 16, 659–670.
(180) Valle, B. C.; Morris, K. F.; Fletcher, K. A.; Fernand, V.; Sword, D. M.;
Eldridge, S.; Larive, C. K.; Warner, I. M. Langmuir 2007, 23, 425–435.
(181) Morgan, E. J.; Rippey, J. M.; Tucker, S. A. Appl. Spectrosc. 2006, 60, 551–
559.
(182) Barrett, E. S.; Dale, T. J.; Rebek, J. J. Am. Chem. Soc. 2007, 129, 3818–
3819.
(183) Schonefeld, K.; Ludwig, R.; Feller, K. H. J. Fluoresc. 2006, 16, 449–454.
(184) Dalgarno, S. J.; Bassil, D. B.; Tucker, S. A.; Atwood, J. L. Angew. Chem.,
Int. Ed. 2006, 45, 7019–7022.
(185) Om, H.; Baker, G. A.; Bright, F. V.; Verma, K. K.; Pandey, S. Chem. Phys.
Lett. 2007, 450, 156–163.
(186) Pallavicini, P.; Diaz-Fernandez, Y. A.; Foti, F.; Mangano, C.; Patroni, S.
Chem.sEur. J. 2007, 13, 178–187.
(187) Ioffe, V. M.; Gorbenko, G. P.; Domanov, Y. A.; Tatarets, A. L.; Patsenker,
L. D.; Terpetsching, E. A.; Dyubko, T. S. J. Fluoresc. 2006, 16, 47–52.
(188) Nishimura, S. Y.; Lord, S. J.; Klein, L. O.; Willets, K. A.; He, M.; Lu, Z. K.;
Twieg, R. J.; Moerner, W. E. J. Phys. Chem. B 2006, 110, 8151–8157.
(189) Gao, F.; Mei, E. W.; Lim, M.; Hochstrasser, R. M. J. Am. Chem. Soc. 2006,
128, 4814–4822.
(190) Margineanu, A.; Hotta, J. I.; Van der Auweraer, M.; Ameloot, M.; Stefan,
A.; Beljonne, D.; Engelborghs, Y.; Herrmann, A.; Muellen, K.; De Schryver,
F. C.; Hofkens, J. Biophys. J. 2007, 93, 2877–2891.
(191) de Almeida, R. F. M.; Borst, J.; Fedorov, A.; Prieto, M.; Visser, A. J. W. G.
Biophys. J. 2007, 93, 539–553.
(192) Benda, A.; Fagul’ova, V.; Deyneka, A.; Enderlein, J.; Hof, M. Langmuir
2006, 22, 9580–9585.
(193) Chiantia, S.; Kahya, N.; Ries, J.; Schwille, P. Biophys. J. 2006, 90, 4500–
4508.
(194) Ries, J.; Schwille, P. Biophys. J. 2006, 91, 1915–1924.
(195) Rhoades, E.; Ramlall, T. F.; Webb, W. W.; Eliezer, D. Biophys. J. 2006,
90, 4692–4700.
(196) Sieber, J. J.; Willig, K. I.; Kutzner, C.; Gerding-Reimers, C.; Harke, B.;
Donnert, G.; Rammner, B.; Eggeling, C.; Hell, S. W.; Grubmuller, H.; Lang,
T. Science 2007, 317, 1072–1076.
(197) Clifford, J. N.; Bell, T. D. M.; Tinnefeld, P.; Heilemann, M.; Melnikov,
S. M.; Hotta, J.; Sliwa, M.; Dedecker, P.; Sauer, M.; Hofkens, J.; Yeow,
E. K. L. J. Phys. Chem. B 2007, 111, 6987–6991.
(198) Fu, Y.; Ye, F. M.; Sanders, W. G.; Collinson, M. M.; Higgins, D. A. J. Phys.
Chem. B 2006, 110, 9164–9170.
(199) Zurner, A.; Kirstein, J.; Doblinger, M.; Brauchle, C.; Bein, T. Nature 2007,
450, 705–708.
LOW-TEMPERATURE LUMINESCENCE
(200) Zhang, Y. X.; Aslan, K.; Malyn, S. N.; Geddes, C. D. Chem. Phys. Lett.
2006, 427, 432–437.
(201) Zhang, Y. X.; Aslan, K.; Previte, M. J. R.; Geddes, C. D. Chem. Phys. Lett.
2006, 432, 528–532.
(202) Wasserberg, D.; Meskers, S. C. J.; Janssen, R. A. J.; Mena-Osteritz, E.;
Bauerle, P. J. Am. Chem. Soc. 2006, 128, 17007–17017.
(203) Sardar, P. S.; Maity, S. S.; Ghosh, S.; Chatterjee, J.; Maiti, T. K.; Dasgupta,
S. J. Phys. Chem. B 2006, 110, 21349–21356.
(204) Richter, M. F.; Baier, J.; Prem, T.; Oellerich, S.; Francia, F.; Venturoli, G.;
Oesterhelt, D.; Southall, J.; Cogdell, R. J.; Kohler, J. Proc. Natl. Acad. Sci.
U.S.A. 2007, 104, 6661–6665.
(205) Da Como, E.; Becker, K.; Feldmann, J.; Lupton, J. M. Nano Lett. 2007,
7, 2993–2998.
(206) Yu, S. J.; Gomez, D. G.; Campiglia, A. D. Appl. Spectrosc. 2006, 60, 1174–
1180.
(207) Yu, S.; Goicoechea, H. C.; Campiglia, A. D. Appl. Spectrosc. 2007, 61,
165–170.
(208) Zhang, W.; Lin, D. L.; Zou, Z. X.; Li, Y. Q. Talanta 2007, 71, 1481–1486.
(209) Campiglia, A. D.; Bystol, A. J.; Yu, S. J. Anal. Chem. 2006, 78, 484–492.
(210) Zhang, L.; Aite, S.; Yu, Z. Rev. Sci. Instrum. 2007, 78, 083701.
(211) Pasternak, S.; Perrin, F.; Ciatto, G.; Palancher, H.; Steinmann, R. Rev. Sci.
Instrum. 2007, 78, 075110.
TOTAL LUMINESCENCE AND SYNCHRONOUS
EXCITATION SPECTROSCOPIES AND RELATED
TECHNIQUES
(212) Poulli, K. I.; Mousdis, G. A.; Georgiou, C. A. Anal. Bioanal. Chem. 2006,
386, 1571–1575.
(213) Deepa, S.; Sarathi, R.; Mishra, A. K. Talanta 2006, 70, 811–817.
(214) Divya, O.; Mishra, A. K. Talanta 2007, 72, 43–48.
(215) Hu, Z.; Tong, C. L. Anal. Chim. Acta 2007, 587, 187–193.
(216) Hou, X. L.; Tong, X. F.; Dong, W. J.; Dong, C. A.; Shuang, S. M.
Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 2007, 66, 552–556.
(217) Cui, F. L.; Wang, J. L.; Cui, Y. R.; Li, J. P. Anal. Chim. Acta 2006, 571,
175–183.
(218) Xia, T. T.; Wang, L.; Bian, G. R.; Dong, L.; Hong, S. Microchim. Acta 2006,
154, 309–314.
(219) Karim, M. M.; Jeon, C. W.; Lee, H. S.; Alam, S. M.; Lee, S. H.; Choi, J. H.;
Jin, S. O.; Das, A. K. J. Fluoresc. 2006, 16, 713–721.
(220) Pulgarin, J. A. M.; Molina, A. A.; Lopez, P. F.; Robles, I. S. F. Anal. Chim.
Acta 2007, 583, 55–62.
(221) Diagaradjane, P.; Yaseen, M. A.; Yu, J.; Wong, M. S.; Anvari, B. J. Biomed.
Opt. 2006, 11, 014012.
(222) Liu, Q.; Chen, K.; Martin, M.; Wintenberg, A.; Lenarduzzi, R.; Panjehpour,
M.; Overholt, B. F.; Vo-Dinh, T. Opt. Express 2007, 15, 12583–12594.
(223) Lead, J. R.; De Momi, A.; Goula, G.; Baker, A. Anal. Chem. 2006, 78,
3609–3615.
(224) Nahorniak, M. L.; Booksh, K. S. Analyst 2006, 131, 1308–1315.
(225) Liu, X. L.; Tao, S.; Deng, N. S.; Liu, Y.; Meng, B. J.; Xue, B.; Liu, G. H.
Anal. Chim. Acta 2006, 572, 134–139.
(226) Pistonesi, M. F.; Di Nezio, M. S.; Centurion, M.; Palomeque, M. E.; Lista,
A. G.; Band, B. S. F. Talanta 2006, 69, 1265–1268.
SOLID SURFACE LUMINESCENCE
(227)
(228)
(229)
(230)
(231)
(232)
(233)
(234)
(235)
(236)
(237)
(238)
(239)
(240)
(241)
(242)
(243)
(244)
(245)
(246)
(247)
(248)
Thompson, A. L.; Hurtubise, R. J. Anal. Chim. Acta 2006, 560, 134–142.
Thompson, A. L.; Hurtubise, R. J. Anal. Chim. Acta 2007, 584, 28–36.
Hubbard, S. E.; Hurtubise, R. J. Talanta 2007, 72, 132–139.
Correa, R. A.; Escandar, G. M. Anal. Chim. Acta 2006, 571, 58–65.
Piccirilli, G. N.; Escandar, G. M. Anal. Chim. Acta 2007, 601, 196–203.
Garcia-Reyes, J. F.; Llorent-Martinez, E. J.; Ortega-Barrales, P.; MolinaDiaz, A. Anal. Chim. Acta 2006, 557, 95–100.
Park, H. Y.; Li, H. W.; Yeung, E. S.; Porter, M. D. Langmuir 2006, 22,
4244–4249.
Liu, X.; Wu, Z.; Nie, H.; Liu, Z.; He, Y.; Yeung, E. S. Anal. Chim. Acta
2007, 602, 229–235.
Hollmann, O.; Czeslik, C. Langmuir 2006, 22, 3300–3305.
Rankl, M.; Ruckstuhl, T.; Rabe, M.; Artus, G. R. J.; Walser, A.; Seeger, S.
ChemPhysChem 2006, 7, 837–846.
Rabe, M.; Verdes, D.; Rankl, M.; Artus, G. R. J.; Seeger, S. ChemPhysChem
2007, 8, 862–872.
Pero, J. K.; Haas, E. M.; Thompson, N. L. J. Phys. Chem. B 2006, 110,
10910–10918.
Petrou, P. S.; Mastichiadis, C.; Christofidis, I.; Kakabakos, S. E. Anal. Chem.
2007, 79, 647–653.
Sanchez-Martinez, M. L.; Aguilar-Caballos, M. P.; Gomez-Hens, A. Anal.
Chem. 2007, 79, 7424–7430.
Dufour, E.; Letort, A.; Laguet, A.; Lebecque, A.; Serra, J. N. Anal. Chim.
Acta 2006, 563, 292–299.
Karoui, R.; Cartaud, G.; Dufour, E. J. Agric. Food Chem. 2006, 54, 2027–
2034.
Ruoff, K.; Luginbuhl, W.; Kunzli, R.; Bogdanov, S.; Bosset, J. O.; von der
Ohe, K.; von der Ohe, W.; Amado, R. J. Agric. Food Chem. 2006, 54,
6858–6866.
Karoui, R.; Dufour, E.; Bosset, J. O.; De Baerdemaeker, J. Food Chem.
2007, 101, 314–323.
Karoui, R.; Dufour, E.; Schoonheydt, R.; De Baerdemaeker, J. Food Chem.
2007, 100, 632–642.
Karoui, R.; Dufour, E.; De Baerdemaeker, J. Food Chem. 2007, 104, 409–
420.
Karoui, R.; Schoonheydt, R.; Decuypere, E.; Nicolai, B.; De Baerdemaeker,
J. Anal. Chim. Acta 2007, 582, 83–91.
Sun, X. Y.; Chen, H.; Gao, H.; Guo, X. Q. J. Agric. Food Chem. 2006, 54,
9687–9695.
LUMINESCENCE IN CHROMATOGRAPHY,
ELECTROPHORESIS, AND FLOW SYSTEMS
(249) Jung, B.; Bharadwaj, R.; Santiago, J. G. Anal. Chem. 2006, 78, 2319–
2327.
(250) Jung, B. G.; Zhu, Y. G.; Santiago, J. G. Anal. Chem. 2007, 79, 345–349.
(251) Karlinsey, J. M.; Landers, J. P. Anal. Chem. 2006, 78, 5590–5596.
(252) Emrich, C. A.; Medintz, I. L.; Chu, W. K.; Mathies, R. A. Anal. Chem.
2007, 79, 7360–7366.
(253) Hashimoto, M.; Barany, F.; Soper, S. A. Biosens. Bioelectron. 2006, 21,
1915–1923.
(254) Case, W. S.; Glinert, K. D.; LaBarge, S.; McGown, L. B. Electrophoresis
2007, 28, 3008–3016.
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4571
(255) Arcibal, I. G.; Santillo, M. F.; Ewing, A. G. Anal. Bioanal. Chem. 2007,
387, 51–57.
(256) Huang, B.; Wu, H. K.; Bhaya, D.; Grossman, A.; Granier, S.; Kobilka, B. K.;
Zare, R. N. Science 2007, 315, 81–84.
(257) Duffy, C. F.; MacCraith, B.; Diamond, D.; O’Kennedy, R.; Arriaga, E. A.
Lab Chip 2006, 6, 1007–1011.
(258) Whitmore, C. D.; Hindsgaul, O.; Palcic, M. M.; Schnaar, R. L.; Dovichi,
N. J. Anal. Chem. 2007, 79, 5139–5142.
(259) Simonnet, C.; Groisman, A. Anal. Chem. 2006, 78, 5653–5663.
(260) Shirasaki, Y.; Tanaka, J.; Makazu, H.; Tashiro, K.; Shoji, S.; Tsukita, S.;
Funatsu, T. Anal. Chem. 2006, 78, 695–701.
(261) Kraly, J. R.; Jones, M. R.; Gomez, D. G.; Dickerson, J. A.; Harwood, M. M.;
Eggertson, M.; Paulson, T. G.; Sanchez, C. A.; Odze, R.; Feng, Z. D.; Reid,
B. J.; Dovichi, N. J. Anal. Chem. 2006, 78, 5977–5986.
(262) Sobhani, K.; Fink, S. L.; Cookson, B. T.; Dovichi, N. J. Electrophoresis 2007,
28, 2308–2313.
(263) Harwood, M. M.; Christians, E. S.; Fazal, M. A.; Dovichi, N. J. J. Chromatogr., A 2006, 1130, 190–194.
(264) Agrwal, A.; Zhang, C. Y.; Byassee, L.; Tripp, R. A.; Nie, S. M. Anal. Chem.
2006, 78, 1061–1070.
(265) Pregebon, D.C.; Toner, M.; Dogle, P. S. Science 2007, 315, 1393–1396.
(266) Kuyper, C. L.; Budzinski, K. L.; Lorenz, R. M.; Chiu, D. T. J. Am. Chem.
Soc. 2006, 128, 730–731.
(267) Kuyper, C. L.; Fujimoto, B. S.; Zhao, Y.; Schiro, P. G.; Chiu, D. T. J. Phys.
Chem. B 2006, 110, 24433–24441.
(268) Wirth, M. J.; Legg, M. A. Annu. Rev. Phys. Chem. 2007, 58, 489–510.
(269) Isailovic, S.; Li, H. W.; Yeung, E. S. J. Chromatogr., A 2007, 1150, 259–
266.
(270) Fang, N.; Zhang, H.; Li, J. W.; Li, H. W.; Yeung, E. S. Anal. Chem. 2007,
79, 6047–6054.
(271) Zhong, Z. M.; Geng, M. L. Anal. Chem. 2007, 79, 6709–6717.
(272) Stein, D.; van der Heyden, F. H. J.; Koopmans, W. J. A.; Dekker, C. Proc.
Natl. Acad. Sci. U.S.A. 2006, 103, 15853–15858.
(273) Benninger, R. K. P.; Koc, Y.; Hofmann, O.; Requejo-Isidro, J.; Neil, M. A. A.;
French, P. M. W.; deMello, A. J. Anal. Chem. 2006, 78, 2272–2278.
(274) Santillo, M. F.; Arcibal, I. G.; Ewing, A. G. Lab Chip 2007, 7, 1212–1215.
DYNAMIC LUMINESCENCE MEASUREMENTS
(275) Qiu, W. H.; Zhang, L. Y.; Okobiah, O.; Yang, Y.; Wang, L. J.; Zhong, D. P.;
Zewail, A. H. J. Phys. Chem. B 2006, 110, 10540–10549.
(276) Andreatta, D.; Sen, S.; Lustres, J. L. P.; Kovalenko, S. A.; Ernsting, N. P.;
Murphy, C. J.; Coleman, R. S.; Berg, M. A. J. Am. Chem. Soc. 2006, 128,
6885–6892.
(277) Kaiser, C. M.; Chang, H. C.; Agashe, V. R.; Lakshmipathy, S. K.; Etchells,
S. A.; Hayer-Hartl, M.; Hartl, F. U.; Barral, J. M. Nature 2006, 444, 455–
460.
(278) Jung, J. Y.; Van Orden, A. J. Am. Chem. Soc. 2006, 128, 1240–1249.
(279) Sharma, J.; Tleugabulova, D.; Czardybon, W.; Brennan, J. D. J. Am. Chem.
Soc. 2006, 128, 5496–5505.
(280) Chen, H. M.; Rhoades, E.; Butler, J. S.; Loh, S. N.; Webb, W. W. Proc.
Natl. Acad. Sci. U.S.A. 2007, 104, 10459–10464.
(281) Mukhopadhyay, S.; Krishnan, R.; Lemke, E. A.; Lindquist, S.; Deniz, A. A.
Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 2649–2654.
(282) Hoffmann, A.; Kane, A.; Nettels, D.; Hertzog, D. E.; Baumgartel, P.;
Lengefeld, J.; Reichardt, G.; Horsley, D. A.; Seckler, R.; Bakajin, O.;
Schuler, B. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 105–110.
(283) Merchant, K. A.; Best, R. B.; Louis, J. M.; Gopich, I. V.; Eaton, W. A. Proc.
Natl. Acad. Sci. U.S.A. 2007, 104, 1528–1533.
(284) Liu, H. W.; Zeng, Y. N.; Landes, C. F.; Kim, Y. J.; Zhu, Y. J.; Ma, X. J.; Vo,
M. N.; Musier-Forsyth, K.; Barbara, P. F. Proc. Natl. Acad. Sci. U.S.A.
2007, 104, 5261–5267.
(285) Yu, J.; Xiao, J.; Ren, X. J.; Lao, K. Q.; Xie, X. S. Science 2006, 311, 1600–
1603.
(286) Elf, J.; Li, G. W.; Xie, X. S. Science 2007, 316, 1191–1194.
(287) Arzhantsev, S.; Jin, H.; Ito, N.; Maroncelli, M. Chem. Phys. Lett. 2006,
417, 524–529.
(288) Arzhantsev, S.; Jin, H.; Baker, G. A.; Maroncelli, M. J. Phys. Chem. B 2007,
111, 4978–4989.
(289) Jin, H.; Li, X.; Maroncelli, M. J. Phys. Chem. B 2007, 111, 13473–13478.
(290) Seth, D.; Chakraborty, A.; Setua, P.; Sarkar, N. J. Phys. Chem. B 2007,
111, 4781–4787.
(291) Ito, N.; Richert, R. J. Phys. Chem. B 2007, 111, 5016–5022.
(293) Novo, M.; Felekyan, S.; Seidel, C. A. M.; Al-Soufi, W. J. Phys. Chem. B
2007, 111, 3614–3624.
(294) Neubauer, H.; Gaiko, N.; Berger, S.; Schaffer, J.; Eggeling, C.; Tuma, J.;
Verdier, L.; Seidel, C. A. M.; Griesinger, C.; Volkmer, A. J. Am. Chem.
Soc. 2007, 129, 12746–12755.
(295) Kudryavtsev, V.; Felekyan, S.; Wozniak, A. K.; Konig, M.; Sandhagen, C.;
Kuhnemuth, R.; Seidel, C. A. M.; Oesterhelt, F. Anal. Bioanal. Chem.
2007, 387, 71–82.
(296) Antonik, M.; Felekyan, S.; Gaiduk, A.; Seidel, C. A. M. J. Phys. Chem. B
2006, 110, 6970–6978.
(297) Kalinin, S.; Felekyan, S.; Antonik, M.; Seidel, C. A. M. J. Phys. Chem. B
2007, 111, 10253–10262.
(298) Latychevskaia, T. Y.; Renn, A.; Wild, U. P. J. Lumin. 2006, 118, 111–122.
(299) Forster, M.; Thomsson, D.; Hania, P. R.; Scheblykin, I. G. Phys. Chem.
Chem. Phys. 2007, 9, 761–766.
(300) Tokimoto, T.; Bethea, T. R. C.; Zhou, M.; Ghosh, I.; Wirth, M. J. Appl.
Spectrosc. 2007, 61, 130–137.
(301) Wei, C. Y. J.; Lu, C. Y.; Kim, Y. H.; Vanden Bout, D. A. J. Fluoresc. 2007,
17, 797–804.
(302) Cao, Z. H.; Huang, C. C.; Tan, W. H. Anal. Chem. 2006, 78, 1478–1484.
(303) Fisz, J. J. J. Phys. Chem. A 2007, 111, 8606–8621.
(304) Deng, T.; Li, J.; Jiang, J. H.; Shen, G. L.; Yn, R. Q. Chem.sEur. J. 2007,
13, 7725–7730.
(305) Mestas, S. P.; Sholders, A. J.; Peersen, O. B. Anal. Biochem. 2007, 365,
194–200.
(306) Xu, Y. F.; McCarroll, M. E. J. Photochem. Photobiol., A: Chem. 2007, 187,
139–145.
(307) Xu, Y. F.; McCarroll, M. J. Photochem. Photobiol., A: Chem. 2006, 178,
50–56.
(308) Valle, B. C.; Morris, K. F.; Fletcher, K. A.; Fernand, V.; Sword, D. M.;
Eldridge, S.; Larive, C. K.; Warner, I. M. Langmuir 2007, 23, 425–435.
(309) Kimaru, I. W.; Xu, Y. F.; McCarroll, M. E. Anal. Chem. 2006, 78, 8485–
8490.
(310) Bader, A. N.; Hofman, E. G.; Henegouwen, P.; Gerritsen, H. C. Opt. Express
2007, 15, 6934–6945.
(311) Lokesh, G. L.; Rachamallu, A.; Kumar, G. D. K.; Natarajan, A. Anal.
Biochem. 2006, 352, 135–141.
(312) Li, W.; Wang, K. M.; Tan, W. H.; Ma, C. B.; Yang, X. H. Analyst 2007,
132, 107–113.
CHEMILUMINESCENCE
(313) Chowdhury, M. H.; Aslan, K.; Malyn, S. N.; Lakowicz, J. R.; Geddes, C. D.
J. Fluoresc. 2006, 16, 295–299.
(314) Previte, M. J. R.; Aslan, K.; Malyn, S.; Geddes, C. D. J. Fluoresc. 2006,
16, 641–647.
(315) Aslan, K.; Malyn, S. N.; Geddes, C. D. J. Am. Chem. Soc. 2006, 128, 13372–
13373.
(316) Previte, M. J. R.; Aslan, K.; Malyn, S. N.; Geddes, C. D. Anal. Chem. 2006,
78, 8020–8027.
(317) Previte, M. J. R.; Geddes, C. D. J. Fluoresc. 2007, 17, 279–287.
(318) Previte, M. J. R.; Aslan, K.; Geddes, C. D. Anal. Chem. 2007, 79, 7042–
7052.
(319) Chowdhury, M. H.; Malyn, S. N.; Aslan, K.; Lakowicz, J. R.; Geddes, C. D.
Chem. Phys. Lett. 2007, 435, 114–118.
(320) Chowdhury, M. H.; Malyn, S. N.; Aslan, K.; Lakowicz, J. R.; Geddes, C. D.
J. Phys. Chem. B 2006, 110, 22644–22651.
(321) Previte, M. J. R.; Geddes, C. D. J. Am. Chem. Soc. 2007, 129, 9850–9851.
(322) Ou, M. G.; Lu, G. W.; Shen, H.; Descamps, A.; Marquette, C. A.; Blum,
L. J.; Ledoux, G.; Roux, S.; Tillement, O.; Cheng, B. L.; Perriat, P. Adv.
Funct. Mater. 2007, 17, 1903–1909.
(323) Wang, X.; Na, N.; Zhang, S. C.; Wu, Y. Y.; Zhang, X. R. J. Am. Chem. Soc.
2007, 129, 6062–6063.
(324) Lee, D.; Khaja, S.; Velasquez-Castano, J. C.; Dasari, M.; Sun, C.; Petros,
J.; Taylor, W. R.; Murthy, N. Nat. Mater. 2007, 6, 765–769.
(325) Jie, G. F.; Liu, B.; Pan, H. C.; Zhu, J. J.; Chen, H. Y. Anal. Chem. 2007,
79, 5574–5581.
(326) Zhang, Y.; Phillips, G. J.; Yeung, E. S. Anal. Chem. 2007, 79, 5373–5381.
(327) Hvastkovs, E. G.; So, M.; Krishnan, S.; Bajrami, B.; Tarun, M.; Jansson,
I.; Schenkman, J. B.; Rusling, J. F. Anal. Chem. 2007, 79, 1897–1906.
(328) Zhan, W.; Bard, A. J. Anal. Chem. 2007, 79, 459–463.
(329) Hewage, H. S.; Wallace, K. J.; Anslyn, E. V. Chem. Commun. 2007, 3909–
3911.
FLUORESCENCE POLARIZATION, MOLECULAR
DYNAMICS, AND RELATED PHENOMENA
NEAR-INFRARED FLUORESCENCE
(292) Widengren, J.; Kudryavtsev, V.; Antonik, M.; Berger, S.; Gerken, M.; Seidel,
C. A. M. Anal. Chem. 2006, 78, 2039–2050.
(330) Tanaka, E.; Ohnishi, S.; Laurence, R. G.; Choi, H. S.; Humblet, V.;
Frangioni, J. V. J. Urol. 2007, 178, 2197–2202.
4572
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
(331) Xu, H.; Baidoo, K.; Gunn, A. J.; Boswell, C. A.; Milenic, D. E.; Choyke,
P. L.; Brechbiel, M. W. J. Med. Chem. 2007, 50, 4759–4765.
(332) Cheng, Z.; Levi, J.; Xiong, Z. M.; Gheysens, O.; Keren, S.; Chen, X. Y.;
Gambhir, S. S. Bioconjugate Chem. 2006, 17, 662–669.
(333) Li, C.; Greenwood, T. R.; Bhujwalla, Z. M.; Glunde, K. Org. Lett. 2006, 8,
3623–3626.
(334) Kalchenko, V.; Shivtiel, S.; Malina, V.; Lapid, K.; Haramati, S.; Lapidot, T.;
Brill, A.; Harmelin, A. J. Biomed. Opt. 2006, 11, 050507.
(335) Leevy, W. M.; Gammon, S. T.; Jiang, H.; Johnson, J. R.; Maxwell, D. J.;
Jackson, E. N.; Marquez, M.; Piwnica-Worms, D.; Smith, B. D. J. Am.
Chem. Soc. 2006, 128, 16476–16477.
(336) Yang, Z.; Zheng, S. Y.; Harrison, W. J.; Harder, J.; Wen, X. X.; Gelovani,
J. G.; Qiao, A.; Li, C. Biomacromolecules 2007, 8, 3422–3428.
(337) Ye, Y. P.; Bloch, S.; Xu, B. G.; Achilefu, S. J. Med. Chem. 2006, 49, 2268–
2275.
(338) Jeng, E. S.; Moll, A. E.; Roy, A. C.; Gastala, J. B.; Strano, M. S. Nano Lett.
2006, 6, 371–375.
(339) Cherukuri, P.; Gannon, C. J.; Leeuw, T. K.; Schmidt, H. K.; Smalley, R. E.;
Curley, S. A.; Weisman, R. B. Proc. Natl. Acad. Sci. U.S.A. 2006, 103,
18882–18886.
(340) Hwang, E. S.; Cao, C. F.; Hong, S. H.; Jung, H. J.; Cha, C. Y.; Choi, J. B.;
Kim, Y. J.; Baik, S. Nanotechnology 2006, 17, 3442–3445.
(341) Zhu, X. J.; Fu, S. T.; Wong, W. K.; Guo, H. P.; Wong, W. Y. Angew. Chem.,
Int. Ed. 2006, 45, 3150–3154.
(342) Mei, Y. J.; Bentley, P. A.; Wang, W. Tetrahedron Lett. 2006, 47, 2447–
2449.
(343) Kiyose, K.; Kojima, H.; Urano, Y.; Nagano, T. J. Am. Chem. Soc. 2006,
128, 6548–6549.
(344) Zhao, W. L.; Carreira, E. M. Chem.sEur. J. 2006, 12, 7254–7263.
(345) McDonnell, S. O.; O’Shea, D. F. Org. Lett. 2006, 8, 3493–3496.
(346) Tang, B.; Zhang, L.; Xu, K. H. Talanta 2006, 68, 876–882.
(347) Sunahara, H.; Urano, Y.; Kojima, H.; Nagano, T. J. Am. Chem. Soc. 2007,
129, 5597–5604.
(348) Bouteiller, C.; Clave, G.; Bernardin, A.; Chipon, B.; Massonneau, M.;
Renard, P. Y.; Romieu, A. Bioconjugate Chem. 2007, 18, 1303–1317.
(349) Verdree, V. T.; Pakhomov, S.; Su, G.; Allen, M. W.; Countryman, A. C.;
Hammer, R. P.; Soper, S. A. J. Fluoresc. 2007, 17, 547–563.
(350) Basheer, M. C.; Santhosh, U.; Alex, S.; Thomas, K. G.; Suresh, C. H.; Das,
S. Tetrahedron 2007, 63, 1617–1623.
(351) Fu, N. N.; Zhang, H. S.; Ma, M.; Wang, H. Electrophoresis 2007, 28, 822–
829.
(352) Ohnmacht, C. M.; Schiel, J. E.; Hage, D. S. Anal. Chem. 2006, 78, 7547–
7556.
(353) Baek, N. S.; Kim, Y. H.; Roh, S. G.; Kwak, B. K.; Kim, H. K. Adv. Funct.
Mater. 2006, 16, 1873–1882.
(354) Arunkumar, E.; Fu, N.; Smith, B. D. Chem.sEur. J. 2006, 12, 4684–4690.
(355) Umezawa, K.; Citterio, D.; Suzuki, K. Chem. Lett. 2007, 36, 1424–1425.
(356) Thomas, J.; Sherman, D. B.; Amiss, T. J.; Andaluz, S. A.; Pitner, J. B.
Bioconjugate Chem. 2007, 18, 1841–1846.
(357) Strekowski, L.; Lee, H.; Mason, J. C.; Say, M.; Patonay, G. J. Heterocycl.
Chem. 2007, 44, 475–477.
(358) Wang, W.; Ke, S.; Kwon, S.; Yallampalli, S.; Cameron, A. G.; Adams, K. E.;
Mawad, M. E.; Sevick-Muraca, E. M. Bioconjugate Chem. 2007, 18, 397–
402.
LUMINESCENCE TECHNIQUES IN BIOLOGICAL
AND CLINICAL ANALYSIS
(359) Hell, S. W. Science 2007, 316, 1153–1158.
(360) Willig, K. I.; Harke, B.; Medda, R.; Hell, S. W. Nat. Methods 2007, 4,
915–918.
(361) Bates, M.; Huang, B.; Dempsey, G. T.; Zhuang, X. W. Science 2007, 317,
1749–1753.
(362) Kural, C.; Serpinskaya, A. S.; Chou, Y. H.; Goldman, R. D.; Gelfand, V. I.;
Selvin, P. R. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 5378–5382.
(363) Elf, J.; Li, G. W.; Xie, X. S. Science 2007, 316, 1191–1194.
(364) Stone, M. D.; Mihalusova, M.; O’Connor, C. M.; Prathapam, R.; Collins,
K.; Zhuang, X. W. Nature 2007, 446, 458–461.
(365) Tokimoto, T.; Bethea, T. R. C.; Zhou, M.; Ghosh, I.; Wirth, M. J. Appl.
Spectrosc. 2007, 61, 130–137.
(366) Baumgart, T.; Hammond, A. T.; Sengupta, P.; Hess, S. T.; Holowka, D. A.;
Baird, B. A.; Webb, W. W. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 3165–
3170.
(367) He, W.; Wang, H. F.; Hartmann, L. C.; Cheng, J. X.; Low, P. S. Proc. Natl.
Acad. Sci. U.S.A. 2007, 104, 11760–11765.
(368) Rosch, P.; Harz, M.; Peschke, K. D.; Ronneberger, O.; Burkhardt, H.;
Schule, A.; Schmauz, G.; Lankers, M.; Hofer, S.; Thiele, H.; Motzkus, H. W.;
Popp, J. Anal. Chem. 2006, 78, 2163–2170.
(369) Adams, K. E.; Ke, S.; Kwon, S.; Liang, F.; Fan, Z.; Lu, Y.; Hirschi, K.;
Mawad, M. E.; Barry, M. A.; Sevick-Muraca, E. M. J. Biomed. Opt. 2007,
12.
(370) Joshi, A.; Bangerth, W.; Sevick-Muraca, E. M. Opt. Express 2006, 14, 6516–
6534.
(371) Chang, S. K.; Marin, N.; Follen, M.; Richards-Kortum, R. J. Biomed. Opt.
2006, 11.
(372) Marin, N. M.; MacKinnon, N.; MacAulay, C.; Chang, S. K.; Atkinson, E. N.;
Cox, D.; Serachitopol, D.; Pikkula, B.; Follen, M.; Richards-Kortum, R.
J. Biomed. Opt. 2006, 11.
(373) Liu, Q.; Chen, K.; Martin, M.; Wintenberg, A.; Lenarduzzi, R.; Panjehpour,
M.; Overholt, B. F.; Vo-Dinh, T. Opt. Express 2007, 15, 12583–12594.
(374) Alimova, A.; Katz, A.; Sriramoju, V.; Budansky, Y.; Bykov, A. A.; Zeylikovich,
R.; Alfano, R. R. J. Biomed. Opt. 2007, 12.
(375) Wang, G. F.; Platz, C. P.; Geng, M. L. Appl. Spectrosc. 2006, 60, 545–
550.
(376) Jo, J. A.; Fang, Q.; Papaioannou, T.; Baker, J. D.; Dorafshar, A. H.; Reil,
T.; Qiao, J. H.; Fishbein, M. C.; Freischlag, J. A.; Marcu, L. J. Biomed.
Opt. 2006, 11.
(377) Scepanovic, O. R.; Fitzmaurice, M.; Gardecki, J. A.; Angheloiu, G. O.;
Awasthi, S.; Motz, J. T.; Kramer, J. R.; Dasari, R. R.; Feld, M. S. J. Biomed.
Opt. 2006, 11.
(378) Zhang, X. A.; Lovejoy, K. S.; Jasanoff, A.; Lippard, S. J. Proc. Natl. Acad.
Sci. U.S.A. 2007, 104, 10780–10785.
(379) Wang, L.; Tan, W. H. Nano Lett. 2006, 6, 84–88.
(380) Chu, T. C.; Shieh, F.; Lavery, L. A.; Levy, M.; Richards-Kortum, R.; Korgel,
B. A.; Ellington, A. D. Biosens. Bioelectron 2006, 21, 1859–1866.
(381) Herr, J. K.; Smith, J. E.; Medley, C. D.; Shangguan, D. H.; Tan, W. H.
Anal. Chem. 2006, 78, 2918–2924.
REAGENTS AND PROBES
(382) Ray, K.; Badugu, R.; Lakowicz, J. R. J. Phys. Chem. B 2006, 110, 13499–
13507.
(383) Ray, K.; Badugu, R.; Lakowicz, J. R. Langmuir 2006, 22, 8374–8378.
(384) Fu, Y.; Lakowicz, J. R. J. Phys. Chem. B 2006, 110, 22557–22562.
(385) Ray, K.; Badugu, R.; Lakowicz, J. R. Chem. Mater. 2007, 19, 5902–5909.
(386) Zhang, J.; Fu, Y.; Lakowicz, J. R. Bioconjugate Chem. 2007, 18, 800–805.
(387) Zhang, J.; Fu, Y.; Lakowicz, J. R. Opt. Express 2007, 15, 13415–13420.
(388) Aslan, K.; Wu, M.; Lakowicz, J. R.; Geddes, C. D. J. Fluoresc. 2007, 17,
127–131.
(389) Wang, L.; Tan, W. H. Nano Lett. 2006, 6, 84–88.
(390) Wu, C. L.; Zheng, J. S.; Huang, C. B.; Lai, J. P.; Li, S. Y.; Chen, C.; Zhao,
Y. B. Angew. Chem., Int. Ed. 2007, 46, 5393–5396.
(391) Senarath-Yapa, M. D.; Phimphivong, S.; Coym, J. W.; Wirth, M. J.;
Aspinwall, C. A.; Saavedra, S. S. Langmuir 2007, 23, 12624–12633.
(392) Smith, J. E.; Wang, L.; Tan, W. T. TrAC, Trends Anal. Chem. 2006, 25,
848–855.
(393) Herr, J. K.; Smith, J. E.; Medley, C. D.; Shangguan, D. H.; Tan, W. H.
Anal. Chem. 2006, 78, 2918–2924.
(394) Smith, J. E.; Medley, C. D.; Tang, Z. W.; Shangguan, D.; Lofton, C.; Tan,
W. H. Anal. Chem. 2007, 79, 3075–3082.
(395) Sathe, T. R.; Agrawal, A.; Nie, S. M. Anal. Chem. 2006, 78, 5627–5632.
(396) Gao, J. H.; Zhang, B.; Gao, Y.; Pan, Y.; Zhang, X. X.; Xu, B. J. Am. Chem.
Soc. 2007, 129, 11928–11935.
(397) Gao, J. H.; Li, L.; Ho, P. L.; Mak, G. C.; Gu, H. W.; Xu, B. Adv. Mater.
2006, 18, 3145–3148.
(398) Talanov, V. S.; Regino, C. A. S.; Kobayashi, H.; Bernardo, M.; Choyke,
P. L.; Brechbiel, M. W. Nano Lett. 2006, 6, 1459–1463.
(399) Hess, S. T.; Girirajan, T. P. K.; Mason, M. D. Biophys. J. 2006, 91, 4258–
4272.
(400) Betzig, E.; Patterson, G. H.; Sougrat, R.; Lindwasser, O. W.; Olenych, S.;
Bonifacino, J. S.; Davidson, M. W.; Lippincott-Schwartz, J.; Hess, H. F.
Science 2006, 313, 1642–1645.
(401) Bates, M.; Huang, B.; Dempsey, G. T.; Zhuang, X. W. Science 2007, 317,
1749–1753.
(402) Bock, H.; Geisler, C.; Wurm, C. A.; Von Middendorff, C.; Jakobs, S.;
Schonle, A.; Egner, A.; Hell, S. W.; Eggeling, C. Appl. Phys. B: Lasers Opt.
2007, 88, 161–165.
(403) Shroff, H.; Galbraith, C. G.; Galbraith, J. A.; White, H.; Gillette, J.; Olenych,
S.; Davidson, M. W.; Betzig, E. Proc. Natl. Acad. Sci. U.S.A. 2007, 104,
20308–20313.
(404) Marti, A. A.; Jockusch, S.; Stevens, N.; Ju, J. Y.; Turro, N. J. Acc. Chem.
Res. 2007, 40, 402–409.
(405) Conley, N. R.; Pomerantz, A. K.; Wang, H.; Twieg, R. J.; Moerner, W. E.
J. Phys. Chem. B 2007, 111, 7929–7931.
(406) Lee, J. Y.; Li, J. W.; Yeung, E. S. Anal. Chem. 2007, 79, 8083–8089.
(407) Seferos, D. S.; Giljohann, D. A.; Hill, H. D.; Prigodich, A. E.; Mirkin, C. A.
J. Am. Chem. Soc. 2007, 129, 15477–15479.
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
4573
(408) Aslan, K.; Malyn, S. N.; Geddes, C. D. Biochem. Biophys. Res. Commun.
2006, 348, 612–617.
(409) Aslan, K.; Malyn, S. N.; Bector, G.; Geddes, C. D. Analyst 2007, 132,
1122–1129.
(410) Schaferling, M.; Wolfbeis, O. S. Chem.sEur. J. 2007, 13, 4342–4349.
(411) Sculimbrene, B. R.; Imperiali, B. J. Am. Chem. Soc. 2006, 128, 7346–
7352.
4574
Analytical Chemistry, Vol. 80, No. 12, June 15, 2008
(412) Poupart, S.; Boudou, C.; Peixoto, P.; Massonneau, M.; Renard, P. Y.;
Romieu, A. Org. Biomol. Chem. 2006, 4, 4165–4177.
(413) Suzuki, Y.; Yokoyama, K.; Namatame, I. Electrophoresis 2006, 27, 3332–
3337.
(414) Klinker, C. C.; Bowser, M. T. Anal. Chem. 2007, 79, 8747–8754.
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