Geddes Reviews in Fluorescence 2008

2010
ISBN: 978-1-4419-1260-2
Verlag: Springer US
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 2008, 490 Seiten

Reihe: Reviews in Fluorescence

This volume serves as a comprehensive collection of current trends and emerging hot topics in the field of fluorescence spectroscopy. It summarizes the year's progress in fluorescence and its applications as well as includes authoritative analytical reviews.

Dr. Chris D. Geddes, Ph.D., Professor, has extensive experience in fluorescence spectroscopy, particularly in fluorescence sensing and metal-fluorophore interactions (Metal-Enhanced Fluorescence), publishing over 190 papers and 18 books. Dr. Geddes is internationally known in fluorescence. He is the editor-in-chief of the Journal of Fluorescence and founding editor of the Who's Who in Fluorescence and Annual Reviews in Fluorescence volumes. In addition, due to the labs pioneering efforts in the fields of metallic nanoparticle-fluorophore interactions, Dr. Geddes recently launched a new Springer Journal, Plasmonics, as well as a new annual hard bound book series Annual Reviews in Plasmonics. Dr. Geddes is Director of the Institute of Fluorescence, within the Medical Biotechnology Center which focuses on the nano-bio-technological applications of fluorescence. Dr. Geddes is currently the chair of 1 NIH study section, a frequent member of the NIBIB special emphasis sensing panels and a permanent member of the NIH EBT study section. http://theinstituteoffluorescence.com/

Autoren/Hrsg.

Geddes, Chris D.

Inhaltsverzeichnis

1;Preface;5
2;Contents;6
3;Contributors;8
4;Fluorescence Anisotropy to Study the Preferential Orientation of Fluorophores in Ordered Bi-Dimensional Systems: Rhodamine 6G/Laponite Layered Films;13
4.1;1 Introduction;13
4.2;2 Fluorescence Anisotropy in Ordered Bi-Dimensional Systems;15
4.3;3 Dye/Clay Systems: Film Characterization;22
4.4;4 Dye Orientation in Ordered Clay Films. A Fluorescence Anisotropy Study;30
4.5;5 Conclusions;41
4.6;References;41
5;Room Temperature Tryptophan Phosphorescence of Proteins in the Composition of Biological Membranes and Solutions;48
5.1;1 Introduction;48
5.2;2 Room Temperature Tryptophan Phosphorescence of Proteins of Isolated Human Erythrocyte Membranes;52
5.3;3 Room Temperature Tryptophan Phosphorescence of Plant Lectins in Solution;60
5.3.1;3.1 Concanavalin A (Con A);61
5.3.2;3.2 Phytohemagglutinin-L (PHA-L);65
5.3.3;3.3 Wheat Germ Agglutinin (WGA);68
5.3.4;3.4 Peanut Agglutinin (PNA);69
5.3.5;3.5 Pisum sativum Agglutinin (PSA);70
5.3.6;3.6 Sambucus nigra Agglutinin (SNA-I);72
5.3.7;3.7 Laburnum anagyroides Lectin (LAL);72
5.3.8;3.8 Solanum tuberosum Agglutinin (STA);72
5.4;References;74
6;Rational Design of FRET-Based Sensor Proteins;79
6.1;1 Introduction;79
6.2;2 Factors That Affect the Ratiometric Change in FRET-Based Sensor Proteins;81
6.3;3 Quantitative Understanding of Energy Transfer by Modeling the Conformational Behavior of Flexible Linkers;83
6.4;4 Quantitative Understanding of the Effect of Flexible Peptide Linkers on Effective Concentration;86
6.5;5 Chelating Fluorescent Protein Chimeras as Efficient Zn(II) Sensor Proteins;89
6.6;6 Taking Advantage of Stickiness: FRET Sensor Proteins Based on Conformational Switching;93
6.7;7 Conclusion and Outlook;95
6.8;References;96
7;Fluorescence Imaging of Calcium Loading and Mitochondrial Depolarization in Cancer Cells Exposed to Heat Stress;98
7.1;1 Introduction;99
7.2;2 Fluorescence Imaging of Mitochondrial Calcium Loading;100
7.2.1;2.1 The Role of Ca 2+ Inside Cells;100
7.2.1.1;2.1.1 Fluorescent Ca 2+ Indicators;103
7.2.2;2.2 Materials and Methods;104
7.3;3 Results;107
7.3.1;3.1 Cell Viability;107
7.3.2;3.2 Visual Evaluation of Fluorescent Ca 2+ Indicators;108
7.3.3;3.3 Fluorescence Imaging of Mitochondrial Transmembrane Potential;111
7.4;4 Discussion;119
7.5;5 Conclusions;121
7.6;References;123
8;Energy Transfer in Silica Nanoparticles: An Essential Toolfor the Amplification of the Fluorescence Signal;128
8.1;1 Introduction;128
8.2;2 The Principles of Energy Transfer Processes;129
8.3;3 The Power of Energy Transfer Processes;131
8.4;4 The Synthesis of Luminescent Silica Nanoparticles;133
8.5;5 Photophysical Properties of Luminescent Silica Nanoparticles;135
8.6;6 Conclusions;144
8.7;References;144
9;Spectroscopic Characterization of Plasma -- Chemically Functionalized and Fluorophore-Labeled Polymer Surfaces;147
9.1;1 Introduction;147
9.2;2 Surface Modification;149
9.2.1;2.1 Surface Functionalization of Polypropylene;149
9.2.2;2.2 Determination of Surface Functionalities with XPS;149
9.2.3;2.3 Fluorophore Labeling of PP Surfaces;150
9.3;3 Characterization of PP Films with Commonly Used Surface-Sensitive Techniques;153
9.4;4 Fluorescence-Based Characterization of Labeled PP Surfaces Pitfalls and Troubleshooting;155
9.4.1;4.1 Environment-Dependent Spectroscopic Properties;155
9.4.2;4.2 Spectral Correction;157
9.4.3;4.3 Reproducibility;157
9.4.4;4.4 Nonspecific Adsorption;158
9.4.5;4.5 Correlation of Fluorescence Measurements and XPS Characterization;160
9.4.6;4.6 Chromogenic and Fluorogenic Labels;161
9.5;5 Summary;164
9.6;References;164
10;Fluorescent Labeling and Its Effect on Hybridization of Oligodeoxyribonucleotides;169
10.1;1 Introduction;169
10.2;2 Fluorophores;170
10.2.1;2.1 General Characteristics of a Fluorophore;171
10.2.2;2.2 Synthesis of Fluorophores;171
10.2.2.1;2.2.1 4-Nitroacenaphthene (I);172
10.2.2.2;2.2.2 4-Nitro-1,8-naphthalic Anhydride or 6-Nitro-benzo[de]isochromene-1,3-dione (II);173
10.2.2.3;2.2.3 4-Amino-1,8-naphthalic Anhydride or 6-Amino-benzo[de]isochromene-1,3-dione (III);173
10.2.2.4;2.2.4 4-Nitro-1,8-naphthalimido- N -caproic Acid or 6-(6-Nitro-1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)-hexanoic Acid (IV);175
10.2.2.5;2.2.5 4-Amino-1,8-naphthalimido- N -caproic Acid or 6-(6-Amino-1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)-hexanoic Acid (V);175
10.2.2.6;2.2.6 6-(6-Isobutyrylamino-1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)- hexanoic Acid (1) ;175
10.2.2.7;2.2.7 6-(6-Dimethylamino-1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)- hexanoic Acid (2) ;177
10.2.2.8;2.2.8 6-(6-Benzoylamino-1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)- hexanoic Acid (3) ;177
10.2.2.9;2.2.9 6-(6-Amino-1-oxo-1H,3H-benzo[de]isoquinolin-2-yl)-hexanoic Acid (4);177
10.2.2.10;2.2.10 6-(6-Amino-1H,3H-benzo[de]isoquinolin-2-yl)-hexanoic Acid (5);178
10.2.3;2.3 Fluorescence Studies on Fluorophores 1--5;178
10.3;3 Synthesis of Fluorescently Labeled Nucleosides and Nucleotides;181
10.3.1;3.1 Generation of Linker Molecule at Nucleosides;181
10.3.1.1;3.1.1 5-(9-Fluorenylmethoxycarbonyl) Aminopentanol-1;182
10.3.1.2;3.1.2 5-[5- N -(9-Fluorenylmethoxycarbonyl)-aminopentanoxy] Uracil and 5-[5- N -(9-Fluorenylmethoxycarbonyl)-aminopentanoxy]-2 -deoxyuridine (7);183
10.3.1.3;3.1.3 5-[5- N- (9-Fluorenylmethoxycarbonyl)-aminopentanoxy] Uracil (2 0 ,3 0 ,5 0 -tri- O -benzoyl-0- d -ribofuranose) (8);183
10.3.1.4;3.1.4 5 0 - O -Dimethoxytrityl-4- N -(tris-4,9,13-triazatridecane-1-yl)-2 0 - deoxycytidine (9) ;183
10.3.2;3.2 Attachment of Fluorophore at Linker Arms of Nucleosides;187
10.3.3;3.3 Synthesis of Labeled Phosphoramidites (10, 11, and 12);188
10.3.4;3.4 Fluorescence Studies on Labelled Nucleosides and Their Phosphoramidites;189
10.4;4 Synthesis of Fluorescently Labeled Oligonucleotides;189
10.4.1;4.1 Labeling of Oligodeoxyribonucleotides Using Post-synthetic Modification Approach;190
10.4.2;4.2 Labeling of Oligodeoxyribonucleotides Using Pre-modification Approach;194
10.4.3;4.3 Hybridization and Fluorescence Studies on Labeled Oligodeoxyribonucleotides;195
10.4.4;4.4 Identification and Electrophoretic Mobility of Labeled Oligodeoxyribonucleotides;199
10.5;5 Conclusion;200
10.6;References;200
11;New Method for Determining Histamine Rate in Halieutic Products;203
11.1;1 Introduction;204
11.2;2 Experimental Study;206
11.2.1;2.1 Products Used;206
11.2.2;2.2 Instrumentation;206
11.2.3;2.3 Experimental Process;207
11.2.3.1;2.3.1 Preparation of Solutions;207
11.2.3.2;2.3.2 Preparation of Samples;207
11.2.3.3;2.3.3 Measurement of Fluorescence;207
11.3;3 Experimental Process;208
11.3.1;3.1 Optimization of Repetitive Dosage;208
11.3.1.1;3.1.1 Verification of the Effect of NaOH Concentration on the Formation of OPA--Histamine Complex by Repetitive Measurement;208
11.3.1.2;3.1.2 The Effect of Temperature, Formation Kinetics of OPA-- NaOH Complex;209
11.3.1.3;3.1.3 The Effect of NaCl Concentration on Fluorescence of OPA--Histamine Complex in Basic Medium;211
11.3.1.4;3.1.4 The Effect of pH on Fluorescence of OPA--Histamine Complex in Basic and Acid Medium;212
11.3.2;3.2 Optimization with Phosphate Buffer;219
11.3.2.1;3.2.1 Preparation of Phosphate Buffer Solution;219
11.3.2.2;3.2.2 Standard Straight line Calibration and Calculation of Detection Limits and Quantification;222
11.3.2.3;3.2.3 Determination of the Recovery by Our Experimental Method;223
11.3.3;3.3 Applications: Determination of Histamine Rate in Fish;223
11.3.3.1;3.3.1 Determination of Histamine Rate in Sample 1;223
11.3.3.2;3.3.2 Determination of Histamine Rate in Sample 2;224
11.4;4 General Conclusion;225
11.5;References;226
12;Spectroscopy of DNAActinomycin Complexes;227
12.1;1 Introduction;227
12.2;2 Emission of 7AAMD in Oligonucleotides and DNA;229
12.3;3 Negligible Energy Transfer from DNA to 7AAMD;231
12.4;4 Estimation of Size of the 7AAMD/HP1 Complex;234
12.5;5 Prompt Binding of 7AAMD to HP1;234
12.6;6 Binding of 7AAMD to DNA;236
12.7;7 Distribution of 7AAMD from HP1 to DNA;237
12.8;8 Caffeine as a Potential Carrier of AMD to DNA;238
12.9;9 Sorption of 7AAMD on Caffeine Clusters;239
12.10;10 Redistribution of 7AAMD from Caffeine Clusters to DNA;242
12.11;11 Conclusion;243
12.12;References;243
13;Fluorescence Spectroscopy in Optoelectronics, Photomedicine, and Investigation of Biomolecular Systems;245
13.1;1 Introduction;245
13.2;2 Fluorescence Spectroscopy as a Tool in Organic Photovoltaics;246
13.2.1;2.1 Fluorescence and Photovoltaics;246
13.2.2;2.2 Fluorescence Quenching -- Donor--Acceptor Pair in Mixed Bimolecular Systems;251
13.2.3;2.3 Fluorescence in Supermolecular Porphyrin--Fullerene Systems;254
13.2.4;2.4 Enhanced Fluorescence -- Dyes in Colloids of Metallic Particles;256
13.3;3 Dye Fluorescence for Medical Photodynamic Study;259
13.3.1;3.1 Spectral Properties of Dyes and their Interactions in Model Systems;260
13.3.2;3.2 Incorporation of Dyes into Cells;264
13.3.3;3.3 Photobleaching Processes vs. Photochemical Reaction;266
13.4;4 Fast Fluorescence for Studying Photosynthetic Organisms, their Fragments and Model Systems;269
13.4.1;4.1 Review the Advanced Techniques of Time-Resolved Fluorescence Quenching;269
13.4.2;4.2 Application of Ultrafast Fluorescence Spectroscopy to the Study of Dynamic Light-Induced Inter- and Intramolecular Deactivation Processes in Molecular Systems;272
13.5;5 Summary;279
13.6;References;279
14;Multicolor Imaging with Fluorescent Proteins in Mice;284
14.1;1 Introduction;284
14.1.1;1.1 GFP and Other Fluorescent Proteins as Imaging Agents;284
14.1.2;1.2 First Use of Fluorescent Proteins in Animals to Visualize Tumor Cells;285
14.1.3;1.3 First Use of Fluorescent Proteins for Whole-Body Imaging;285
14.1.3.1;1.3.1 Whole-Body Imaging of Gene Expression;286
14.1.3.2;1.3.2 Whole-Body Imaging of Angiogenesis;286
14.1.3.3;1.3.3 Whole-Body Imaging of Bacterial Infection;287
14.1.3.4;1.3.4 External Imaging Through Skin Flaps;288
14.1.3.5;1.3.5 Whole-Body Imaging of Graft--Versus-Host Disease;288
14.1.4;1.4 Autofluorescence Is Not a Problem with Fluorescent Protein-Based In Vivo Imaging;288
14.1.5;1.5 Use of Whole-Body Imaging with Fluorescent Proteins to Measure Drug Response in Real Time;289
14.1.6;1.6 Imaging the Relationship of Tumor Cells and Blood Vessels;290
14.1.7;1.7 Visualizing Cellular and Nuclear Deformation and Dynamics in Small Blood Vessels;291
14.1.8;1.8 Imaging Tumor Cell Deformation and Migration in Blood Vessels of Live Mice in Real Time;292
14.1.9;1.9 Color Coding of Cancer Cells Determines Clonality of Metastasis;292
14.1.10;1.10 Imageable Tumor--Host Models;293
14.1.11;1.11 Advantages of GFP Imaging Over Luciferase and Other Optical Imaging Techniques;294
14.1.12;1.12 New Features and Models with Fluorescent Proteins;296
14.1.13;1.13 Advantages of Fluorescent Protein Imaging Over Quantum Dots;297
14.1.14;1.14 Growth of Fluorescent Protein-Expressing Cells in Syngeneic Models: Lack of Apparent Immunological Response;297
14.2;2 Conclusions;298
14.2.1;2.1 Example of the Use of Fluorescent Proteins to Discover Properties of Stem Cells;299
14.2.2;2.2 Future Directions;299
14.2.3;2.3 Multiphoton Imaging;300
14.2.4;2.4 Potential Human Use of Fluorescent Proteins;301
14.3;References;302
15;Genetically Encoded Fluorescent and Bioluminescent Probes for Illuminating Cellular Signaling Pathways;309
15.1;1 Introduction;309
15.2;2 Second Messengers;310
15.2.1;2.1 Nitric Oxide (NO);310
15.2.2;2.2 Inositol 1,4,5-Trisphosphate (IP3);310
15.2.3;2.3 Cyclic GMP;310
15.2.4;2.4 Phosphatidylinositol-3,4,5-trisphosphate (PIP3);313
15.3;3 Fluorescent Indicators for Imaging Protein Phosphorylation;316
15.4;4 ProteinProtein Interactions;317
15.4.1;4.1 Split-GFP is Spliced upon Protein--Protein Interactions;317
15.4.2;4.2 Locating a Protein--Protein Interaction by Split Renilla luciferase Complementation;319
15.5;5 Protein Localization in Organelles;321
15.5.1;5.1 Mitochondria-Targeting Protein;321
15.5.2;5.2 ER-Targeting Protein;322
15.5.3;5.3 Nucleocytoplasmic Trafficking of Functional Proteins;324
15.6;References;326
16;Fluorescent Protein FRET Applications;327
16.1;1 Introduction;327
16.1.1;1.1 FRET Theory;327
16.1.2;1.2 Practical Implications of FRET Theory;328
16.1.3;1.3 Common Applications of FRET;328
16.1.4;1.4 The RRC;329
16.2;2 Fluorescent Protein FRET Pairs;330
16.3;3 Enhancing FRET Through Directed Evolution;331
16.3.1;3.1 Linker Length Optimization;331
16.3.2;3.2 Directed Evolution of the CFP--YFP Pair;332
16.4;4 Using FRET to Screen Libraries;335
16.5;5 Future Opportunities for FRET-Based Screening;336
16.5.1;5.1 Protease Evolution;336
16.5.2;5.2 Protein Interaction Screening;337
16.5.3;5.3 Small Molecule Indicator Development;338
16.5.4;5.4 Long Wavelength FRET Pair Optimization;338
16.6;6 Conclusions;339
16.7;References;339
17;Imaging Protein Interactions in Living Cells Using the Fluorescent Proteins;342
17.1;1 Introduction;342
17.2;2 Spectral Variants of the Fluorescent Proteins;343
17.2.1;2.1 The Red Fluorescent Proteins;345
17.2.2;2.2 The Next Generation of Colors;345
17.2.3;2.3 The Photoactivatable FPs;346
17.3;3 Quantifying the Dynamic Behavior of Proteins;347
17.3.1;3.1 The Biological Model;347
17.3.2;3.2 Fluorescence Recovery After Photobleaching;347
17.3.3;3.3 Photoactivation;348
17.3.4;3.4 Multicolor Imaging of Protein Co-localization;349
17.4;4 Defining the Spatial Relationships Between Proteins;351
17.4.1;4.1 Fluorescence Resonance Energy Transfer;352
17.4.2;4.2 Spectral Bleed-Through Correction;352
17.4.3;4.3 Acceptor Photobleaching;353
17.4.4;4.4 Fluorescence Decay Measurements;355
17.5;5 Conclusions;357
17.6;References;358
18;Engineering Green Fluorescent Proteins Using an Expanded Genetic Code;363
18.1;1 Introduction;364
18.2;2 Major av GFP Classes Generated by Classical Methods;365
18.3;3 Expanded Amino Acid Repertoire in Protein Synthesis;366
18.4;4 Aminotryptophans and Golden Fluorescent Protein;368
18.4.1;4.1 Basic Features and Translational Activity of Aminotryptophans;368
18.4.2;4.2 Engineering Fluorescent Proteins: From Green to Gold;370
18.4.3;4.3 Steady-State and Dynamic Spectroscopic Features of GdFP;371
18.4.4;4.4 Structural Framework of Golden Fluorescence;373
18.4.5;4.5 Monomeric State and Temperature-Dependent Fluorescence in GdFP;375
18.5;5 Chromophores with Amino- and Methoxy-Tyrosines;376
18.6;6 Thieno- and Seleno-Pyroles in av GFP;377
18.7;7 Fluorinated Trp-Residues in av GFP;378
18.7.1;7.1 Global Fluorination of Trp-Residues in Proteins;378
18.7.2;7.2 Fluorinated Trp-Residues in ECFP and EGFP;378
18.7.3;7.3 Fluorinated Trp-Residues as Reporters of Chromophore Dynamics;379
18.8;8 av GFPs with Globally Fluorinated Tyr-Residues;380
18.8.1;8.1 Fluorinated Tyr-Residues as Substrates for Protein Synthesis;380
18.8.2;8.2 Chromophore Fluorination in Ortho- and Meta Positions;380
18.8.3;8.3 Fluorination of the Chromophore Environment in EYFP;385
18.9;9 Perspectives and Outlook;385
18.10;References;387
19;Fluorescent Proteins in Transgenic Plants;391
19.1;1 Introduction;391
19.2;2 FPs in Model Organisms;392
19.3;3 GFP in Transgenic Plants;393
19.4;4 GFP Variants for Plant Expression;393
19.5;5 Other Colors, Other Organisms;394
19.6;6 FP Toxicity and Allergenicity;395
19.7;7 FPs in Plant Research;397
19.8;8 Whole Plant FP Applications;397
19.8.1;8.1 Plant Zygosity Determination Using GFP as a Genetic Marker;397
19.8.2;8.2 Monitoring Transgenic Organisms;398
19.8.3;8.3 Environmental Monitoring;399
19.9;9 Instrumentation and Methods for FP Detection and Quantification in Plants;400
19.9.1;9.1 Visual Detection;400
19.9.2;9.2 Lab-Based FluoroMax-4 Spectrofluorometer;401
19.9.3;9.3 Portable Hand-Held GFP-Meter;401
19.9.4;9.4 Stand-Off Laser-Induced Fluorescence Detection;402
19.10;10 Customized FPs;402
19.11;11 Conclusions;404
19.12;References;404
20;Peptide Foldamers: From Spectroscopic Studies to Applications;408
20.1;1 Introduction;408
20.2;2 Spectroscopic Studies of Foldamer Structure in Solution;410
20.2.1;2.1 Secondary Structure;410
20.2.2;2.2 More than just a Spectroscopic Ruler: FRET as a Structural Technique;413
20.2.3;2.3 Molecular Mechanics Calculations;415
20.2.4;2.4 Validation of the Computed Structures;416
20.3;3 Selected Applications;418
20.3.1;3.1 Peptide Foldamers as Models of Protein Folding;418
20.3.2;3.2 Peptide Foldamers as Building Blocks for Molecular Devices;422
20.4;4 Conclusions;424
20.5;References;424
21;Circularly Polarized Luminescence (CPL) of Proteins and Protein Complexes;428
21.1;1 Introduction: What Is CPL?;429
21.2;2 How to Measure CPL?;431
21.2.1;2.1 Instrumentation;431
21.2.2;2.2 Calibration;434
21.2.3;2.3 Artifacts;435
21.3;3 Circularly Polarized Intrinsic Fluorescence of Proteins;436
21.3.1;3.1 Peptides;436
21.3.2;3.2 Poly(-amino acid);436
21.3.3;3.3 Tyrosine and Tryptophan Residues in Proteins;438
21.3.4;3.4 Complexes of Proteins with Functional Non-fluorescent Agents;442
21.3.5;3.5 Protein Conformation Perturbation;443
21.4;4 Protein Complexes with Fluorescent Agents;444
21.4.1;4.1 Probes;444
21.4.2;4.2 Cofactors and Bilirubin;446
21.4.3;4.3 Lanthanides;449
21.4.4;4.4 Light-Harvesting Chlorophyll--Protein Complex of Photosynthetic Photosystem II (LHCII);452
21.5;5 Conclusions;456
21.6;References;456
22;New Dual Fluorescent Dyes Based on Modified Excited State with Extended Conjunction Photophysical Model;463
22.1;1 Introduction and Background;464
22.1.1;1.1 Internal Calibration of Fluorescence Signal in Microscale Sensor Systems;464
22.1.2;1.2 Summary of Optical Signal Switching Arrangements;465
22.1.3;1.3 OR--OR Switching in a Ground State;467
22.1.4;1.4 OR--OR Switching in a Fast Reversible Excited-State Reaction;469
22.2;2 Results;470
22.3;3 Refined Matrix Results;474
22.4;4 Discussion;476
22.5;References;478
23;Index;480