Analytical Chemistry Chemical Cytometry Quantitates Superoxide

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multicomponent patterned surfaces can be fabricated simply by printing on top of a base film. The two-component structures were shown to be stable to prolonged sonication, indicating covalent coupling of the second modifier to the base layer. The availability of such a method will facilitate application of the aryldiazonium salt surface modification approach in areas such as the fabrication of bio- and chemical sensors. ACKNOWLEDGMENT This work was supported by the MacDiarmid Institute for Advanced Materials and Nanotechnology. J.L. and D.J.G thank the New Zealand Tertiary Education Commission for doctoral scholarships and B.S.F. thanks the Australian Government’s Endeavour Research Fellowship program. We thank Dr. John Loring for use of the Linkfit curve fitting software. 7034 Analytical Chemistry, Vol. 82, No. 16, August 15, 2010 SUPPORTING INFORMATION AVAILABLE Characterizations of the following modified surfaces prepared by printing using nonpatterned stamps: AP on PPF, NP on Au, and NP on HF-treated Si; cyclic voltammograms of CP layers and bare PPF after activation with SOCl2 and reaction with 4-nitroaniline; repeat cyclic voltammograms of a PPF surface bearing a CP film, overprinted with an NP layer; figures of AFM line profiles of data presented in Tables 2 and 3; SEM image of the surface shown in Figure 5. This material is available free of charge via the Internet at http://pubs.acs.org. Received for review July 6, 2010. Accepted July 10, 2010. AC101785C
Anal. Chem. 2010, 82, 7035–7043 Quantitation, Visualization, and Monitoring of Conformational Transitions of Human Serum Albumin by a Tetraphenylethene Derivative with Aggregation-Induced Emission Characteristics Yuning Hong, † Chao Feng, ‡ Yong Yu, †,‡ Jianzhao Liu, † Jacky Wing Yip Lam, † Kathy Qian Luo, ‡,§ and Ben Zhong Tang* ,†,# Nano Science and Technology Program, Department of Chemistry, Institute of Molecular Functional Materials, Bioengineering Program, and Department of Chemical and Biomolecular Engineering, The Hong Kong University of Science and Technology (HKUST), Clear Water Bay, Kowloon, Hong Kong, China, School of Chemical and Biomedical Engineering, Nanyang Technological University, Singapore 637457, and Department of Polymer Science and Engineering, Institute of Biomedical Macromolecules, Key Laboratory of Macromolecular Synthesis and Functionalization of the Ministry of Education, Zhejiang University, Hangzhou 310027, China Human serum albumin (HSA) is a major protein component of blood plasma, and its assay is of obvious value to biological research. We, herein, present a readily accessible fluorescent bioprobe for HSA detection and quantitation. A nonemissive tetraphenylethene derivative named sodium 1,2-bis[4-(3-sulfonatopropoxyl)phenyl]-1,2-diphenylethene (BSPOTPE) is induced to emit by HSA, showing a novel phenomenon of aggregation-induced emission (AIE). The AIE bioprobe enjoys a broad working range (0-100 nM), a low detection limit (down to 1 nM), and a superior selectivity to albumins. The fluorescent bioassay is unperturbed by the miscellaneous bioelectrolytes in the artificial urine. The AIE luminogen can also be used as a rapid and sensitive protein stain in gel electrophoresis for HSA visualization. Utilizing the AIE feature of BSPOTPE and the Förster resonance energy transfer from HSA to BSPOTPE, the unfolding process of HSA induced by guanidine hydrochloride is monitored, which reveals a multistep transition with the involvement of molten globule intermediates. Computational modeling suggests that the AIE luminogens dock in the hydrophobic cleft between subdomains IIA and IIIA of HSA with the aid of hydrophobic effect, charge neutralization, and hydrogen bonding interactions, offering mechanistic insight into the microenvironment inside the hydrophobic cavity. Human serum albumin (HSA) is the most abundant protein in the circulatory system and plays multiple biological functions in the human body. 1 For example, it regulates water balance between blood and tissues and serves as a physiological carrier for various endogenous and exogenous substances that are * To whom correspondence should be addressed. E-mail: tangbenz@ust.hk. † Nano Science and Technology Program, Department of Chemistry, Institute of Molecular Functional Materials, and Bioengineering Program, HKUST. ‡ Department of Chemical and Biomolecular Engineering, HKUST. § Nanyang Technological University. # Zhejiang University. (1) Peters, T., Jr. Adv. Protein Chem. 1985, 37, 161. partially soluble in the bloodstream, such as bilirubin, fatty acids, and drugs. 2-5 The albumin is synthesized in the liver. A low level of albumin in the blood serum, known as hypoproteinemia, may indicate liver failure, cirrhosis, and chronic hepatitis. 6 When blood passes through healthy kidneys, the kidneys filter out waste products but keep the substances the body needs, such as albumin and other proteins. Appearance of an excess amount of proteins in urine is a sign of chronic kidney disease, which may result in diabetes, high blood pressure, and problems associated with inflammation in the kidneys. 7 Many studies have been done on diabetic nephrosis, with microalbuminuria being identified as an early sign. 8 Microalbuminuria is commonly diagnosed by elevated protein concentration (30-300 mg/L) in the urine on at least two occasions. A higher albumin value is regarded as albuminuria. The urine-testing dipsticks impregnated with pH sensitive dyes are normally used for daily health monitoring. 9 The level of albumin caused by microalbuminuria, however, cannot be accurately assayed by the dipsticks due to their low sensitivity. 10 It is, thus, of clinical value to develop effective methods for urinary protein detection and quantitation. Colorimetric methods, such as Brandford and Lowry assays, have traditionally been used for protein quantitation in solutions. 11,12 These methods, however, generally lack sensitivity and accuracy, (2) Carter, D. C.; Ho, J. X. Adv. Protein Chem. 1994, 45, 153. (3) (a) Neuzil, J.; Stocker, R. J. Biol. Chem. 1994, 269, 16712. (b) Hu, Y. J.; Liu, Y.; Xiao, X. H. Biomacromolecules 2009, 10, 517. (4) Berde, C. B.; Hudson, B. S.; Simoni, R. D.; Sklar, L. A. J. Biol. Chem. 1979, 254, 391. (5) Sjoholm, I.; Ekman, B.; Kober, A. Mol. Pharmacol. 1979, 16, 767. (6) Murch, S. H.; Winyard, P. J. D.; Koletzko, S.; Wehner, B.; Cheema, H. A.; Risdon, R. A.; Phillips, A. D.; Meadows, N.; Klein, N. J.; Walker-Smith, J. A. Lancet 1996, 347, 1299. (7) Hoogenberg, K.; Sluiter, W. J.; Dullaart, R. P. F. Acta Endrocrinol. 1993, 129, 151. (8) (a) Mogensen, C. E.; Keane, W. F.; Bennett, P. H.; Jerums, G.; Parving, H. H.; Passa, P.; Steffes, M. W.; Striker, G. E.; Viberti, G. C. Lancet 1995, 346, 1080. (b) Nomata, S.; Haneda, K.; Moriya, T.; Katayama, S.; Iwamoto, Y.; Sakai, H.; Tomino, Y.; Matsuo, S.; Asano, Y.; Makino, H. Jpn. J. Nephrol. 2005, 47, 768. (9) Rose, B. D. Pathophysiology of Renal Disease; McGraw Hill: New York, 1987. (10) Martinez, A. W.; Phillips, S. T.; Butte, M. J.; Whitesides, G. M. Angew. Chem., Int. Ed. 2007, 46, 1318. 10.1021/ac1018028 © 2010 American Chemical Society 7035 Analytical Chemistry, Vol. 82, No. 16, August 15, 2010 Published on Web 07/20/2010
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Anal. Chem. 2010, 82, 6745-6750 Let
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purchased from Invitrogen-Molecular
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Figure 3. Electropherograms of TPP-
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Anal. Chem. 2010, 82, 6751-6755 Res
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(pH 8.0) with cysteine and cystamin
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Figure 4. Ion mobility mass spectra
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GOx glucose + O298 gluconic acid +
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coater at 2000 rpm for 20 s, and th
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Figure 5. Comparison of cyclic volt
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in channels with either no grooves
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indicators of atmospheric processin
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Figure 1. GC/MS total ion chromatog
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Table 2. Concentrations and Stable
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on a substrate are preferred. 20-24
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Figure 4. SERS analysis of NAADP co
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Anal. Chem. 2010, 82, 6775-6781 Hig
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tion, 2 µL of proprionaldehyde wer
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Figure 4. Analysis of 2a by HPLC-MS
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eaction of 1a with PBH can be condu
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Numerous references had demonstrate
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Figure 1. TEM images of the prepare
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Figure 4. Schematic representation
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esult in a big SPR signal change wi
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also reduces chemical noise, which
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Table 1. Extraction Yields, Liquid
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scanning of AMPP amides of the anal
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Anal. Chem. 2010, 82, 6797-6806 δ
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Figure 1. Schematic view of the pre
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from the specimen and enclosed in a
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Figure 4. (A) IRMS mass-44 chromato
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Table 3. Ambient Measurement Result
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Anal. Chem. 2010, 82, 6807-6813 Dir
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Polymerase (1 U per sample). Reacti
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of which was constant for all ampli
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analytically useful signals at less
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carbon black and RP-C18 for the ext
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solution in an equal volume, and 1
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Table 2. Concentrations and Ratios
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Anal. Chem. 2010, 82, 6821-6829 Mac
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mg/mL protein, followed by separati
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Figure 2. Productivity of SEQUST an
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Figure 4. High-resolution MS/MS spe
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Figure 6. Characterization of PSMs
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containing T-T mismatches. 23 Based
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Figure 1. Extinction spectra of sol
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Figure 3. (A) The value of Ex650 nm
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Figure 5. Extinction spectra and co
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wished to explore the dehydration o
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constant medium for separation; we
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Figure 2. Standards of (Pi)n, n ) 1
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Figure 5. Quantitative calibration
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Anal. Chem. 2010, 82, 6847-6853 Met
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Figure 1. 226 Ra spectrum by liquid
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Table 1. Counting Properties and De
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Table 3. Analysis of 226 Ra in Sedi
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mercial microarray scanner and fabr
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Figure 2. Optical transmission meas
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Figure 5. Volcano plots detailing t
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data as well. The 41 genes in Table
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corresponding compound if its chemi
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Figure 1. Schematic illustration of
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Table 1. Absolute Quantification Re
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ment. Therefore, the long-time drea
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Figure 1. Chemically actuated micro
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Figure 2. Influence of a surfactant
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Figure 5. Device to eject and mix s
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Anal. Chem. 2010, 82, 6877-6886 Imm
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NaCl, phosphate buffer saline (PBS)
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Figure 2. Product ion mass spectra
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-70 °C resolved the problem, givin
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Table 1. Intraday Precision and Acc
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Anal. Chem. 2010, 82, 6887-6894 Fer
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Figure 1. Infrared spectra of (A) u
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Figure 3. Cyclic voltammograms obta
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Figure 6. Calculated charge from ch
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Anal. Chem. 2010, 82, 6895-6903 Ele
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Table 1. Chemical Structure, pKa Va
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pH with a tilted baseline (Figure 1
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Table 2. Linearity and Detection Li
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ascorbic acid (AA), uric acid (UA),
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the multielement capabilities, the
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RESULTS AND DISCUSSION Sulfur Detec
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Table 2. Molecular Properties and C
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Anal. Chem. 2010, 82, 6911-6918 Dir
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dilution and hybridization buffer.
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solution under appropriate incubati
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Figure 4. Standardization curve for
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Anal. Chem. 2010, 82, 6919-6925 Ele
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the ×10 objective, to have a large
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Figure 2. With a suitable removal o
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the NB signal in a much better foot
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Scheme 1. Reactions of Selenium Rea
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Figure 2. (a) ESI-MS spectrum showi
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Figure 4. (a) ESI-MS spectrum showi
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Anal. Chem. 2010, 82, 6933-6939 Dif
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trode 28 by a finite element using
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Figure 4. Comparison between simula
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Figure 6. Comparison between simula
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educed in the vicinity of double bo
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Figure 2. Normalized product ion ab
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Figure 4. EID (a) and IRMPD (b) of
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Anal. Chem. 2010, 82, 6947-6957 Ide
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Figure 1. Schematic flowchart showi
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difference, ppm compound Table 1. I
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isoforms, its successful use, in th
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Figure 5. Extracted ion current ESI
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m/z 1172.935 was observed for Ser14
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linked products via affinity tags.
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Scheme 2. Fragmentation Mechanism o
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Figure 1. (A) ESI-LTQ-CID-MS 2 prod
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Figure 3. (A) ESI-LTQ-CID-MS 2 prod
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Figure 5. (A) MALDI-TOF/TOF product
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Anal. Chem. 2010, 82, 6969-6975 Ana
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Figure 3. Equilibrium response as a
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Figure 6. The average measured resp
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for the fill time, and we find that
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nucleotide tails. 3-5 Thus, the amo
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allow the use of higher aptamer con
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quent ligation of the aptamers afte
Page 239 and 240: Anal. Chem. 2010, 82, 6983-6990 Imp
Page 241 and 242: Figure 2. Configuration editor wind
Page 243 and 244: Figure 4. Dependencies between volu
Page 245 and 246: Since the time for liquid expulsion
Page 247 and 248: Anal. Chem. 2010, 82, 6991-6999 Int
Page 249 and 250: Figure 1. Representation of the Car
Page 251 and 252: Table 2. Capillary Electrophoresis
Page 253 and 254: Figure 4. (A) Typical raw electroph
Page 255 and 256: field. DNA profiles were delivered
Page 257 and 258: Another approach to handle this lim
Page 259 and 260: (principal components, PCs) in whic
Page 261 and 262: Figure 5. Relevant score plots and
Page 263 and 264: CONCLUSIONS In this paper we have i
Page 265 and 266: electroactive-species loaded liposo
Page 267 and 268: Figure 2. Qdot-based FLFTS response
Page 269 and 270: Figure 6. Fluorescence imaging of Q
Page 271 and 272: Anal. Chem. 2010, 82, 7015-7020 Sel
Page 273 and 274: Table 1. Effect of 1 D-LC Condition
Page 275 and 276: Figure 3. Peak-production rate vers
Page 277 and 278: Anal. Chem. 2010, 82, 7021-7026 Cel
Page 279 and 280: luciferase (T7 control vector) was
Page 281 and 282: Figure 3. Inhibitory effects of luc
Page 283 and 284: Anal. Chem. 2010, 82, 7027-7034 Pat
Page 285 and 286: Electrochemistry. Electrochemical m
Page 287 and 288: Figure 2. SEM images of Au substrat
Page 289: Table 3. Film Thickness Measurement
Page 293 and 294: Figure 1. (A) FL spectra of BSPOTPE
Page 295 and 296: Figure 4. (A) Variation in the FL i
Page 297 and 298: Figure 6. (A) FL spectra of BSPOTPE
Page 299 and 300: Scheme 1. Proposed Mechanism for Fl
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Page 303 and 304: Figure 2. Free fluorophores do not
Page 305 and 306: Anal. Chem. 2010, 82, 7049-7052 Dev
Page 307 and 308: Figure 2. Comparative analysis of d
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