Using nonfluorescent Förster resonance energy transfer acceptors in protein binding studies

Analytical Biochemistry

Volumn 393, Issue 2, 2009, Pages 196-204

  Ruan, Qiaoqiao ^a   Skinner, Joseph P ^a   Tetin, Sergey Y ^a  

^a ABBOTT DIAGNOSTICS   (United States)

Author keywords

Antibody affinity; Binding kinetics; Black hole quenchers; Fluorescence spectroscopy; FRET; Nonfluorescent FRET acceptors; Protein ligand binding

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; BIOCHEMISTRY; CHROMOPHORES; DISSOCIATION; ENERGY TRANSFER; EQUILIBRIUM CONSTANTS; FLUORESCENCE SPECTROSCOPY; FORSTER RESONANCE ENERGY TRANSFER; KINETICS; MONOCLONAL ANTIBODIES; PROBABILITY DISTRIBUTIONS;

ANTIBODY AFFINITY; BINDING KINETICS; BLACK HOLES; FRET; NONFLUORESCENT FRET ACCEPTORS; PROTEIN LIGANDS;

BINDING ENERGY;

BRAIN NATRIURETIC PEPTIDE; CHORIONIC GONADOTROPIN; IMMUNOGLOBULIN G ANTIBODY; MONOCLONAL ANTIBODY;

ANTIBODY AFFINITY; ARTICLE; BINDING KINETICS; CONCENTRATION PROCESS; CONJUGATION; CONTROLLED STUDY; DISSOCIATION CONSTANT; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN INTERACTION; SENSITIVITY ANALYSIS;

CAPRA HIRCUS; CRICETINAE;

EID: 68349139580     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.06.033     Document Type: Article

References (33)

1. Jameson D.M., and Seifried S.E. Quantification of protein-protein interactions using fluorescence polarization. Methods 19 (1999) 222-233
2. Tetin S.Y., and Hazlett T.L. Optical spectroscopy in studies of antibody-hapten interactions. Methods 20 (2000) 341-361
3. Royer C.A., and Scarlata S.F. Fluorescence approaches to quantifying biomolecular interactions. Methods Enzymol. 450 (2008) 79-106
4. Weljie A.M., and Vogel H.J. Tryptophan fluorescence of calmodulin binding domain peptides interacting with calmodulin containing unnatural methionine analogues. Protein Eng. 13 (2000) 59-66
5. Weber G. Polarization of the fluorescence of macromolecules: II. Fluorescent conjugates of ovalbumin and bovine serum albumin. Biochem. J. 51 (1952) 155-167
6. Visser A.J., and Lee J. Lumazine protein from the bioluminescent bacterium Photobacterium phosphoreum: a fluorescence study of the protein-ligand equilibrium. Biochemistry 19 (1980) 4366-4372
7. Eftink M.R. Fluorescence quenching reactions: probing biological macromolecular structures. In: Dewey T.G. (Ed). Biophysical and Biochemical Aspects of Fluorescence Spectroscopy (1991), Plenum, New York 1-41
8. Tetin S.Y., Swift K.M., and Matayoshi E.D. Measuring antibody affinity and performing immunoassay at the single molecule level. Anal. Biochem. 307 (2002) 84-91
9. Schwille P., Meyer-Almes F.J., and Rigler R. Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys. J. 72 (1997) 1878-1886
10. Ruan Q., and Tetin S.Y. Applications of dual-color fluorescence cross-correlation spectroscopy in antibody binding studies. Anal. Biochem. 374 (2008) 182-195
11. Chen Y., Muller J.D., So P.T., and Gratton E. The photon counting histogram in fluorescence fluctuation spectroscopy. Biophys. J. 77 (1999) 553-567
12. Wu B., and Muller J.D. Time-integrated fluorescence cumulant analysis in fluorescence fluctuation spectroscopy. Biophys. J. 89 (2005) 2721-2735
13. Clegg R.M. Fluorescence resonance energy transfer. Curr. Opin. Biotechnol. 6 (1995) 103-110
14. Forster T. Intermolecular energy migration and fluorescence. Annu. Phys. (Leipzig) 2 (1948) 55-75
15. Steinberg I.Z. Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides. Annu. Rev. Biochem. 40 (1971) 83-114
16. Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47 (1978) 819-846
17. Wu P., and Brand L. Resonance energy transfer: methods and applications. Anal. Biochem. 218 (1994) 1-13
18. Matayoshi E.D., Wang G.T., Krafft G.A., and Erickson J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 247 (1990) 954-958
19. Marcotte P.A., Richardson P.L., Guo J., Barrett L.W., Xu N., Gunasekera A., and Glaser K.B. Fluorescence assay of SIRT protein deacetylases using an acetylated peptide substrate and a secondary trypsin reaction. Anal. Biochem. 332 (2004) 90-99
20. Marras S.A., Kramer F.R., and Tyagi S. Efficiencies of fluorescence resonance energy transfer, contact-mediated quenching in oligonucleotide probes. Nucleic Acids Res. 30 (2002) e122
21. O'Sullivan P.J., Burke M., Soini A.E., and Papkovsky D.B. Synthesis, evaluation of phosphorescent oligonucleotide probes for hybridisation assays. Nucleic Acids Res. 30 (2002) e114
22. Adamczyk M., Moore J.A., and Shreder K. Quenching of biotinylated aequorin bioluminescence by dye-labeled avidin conjugates: application to homogeneous bioluminescence resonance energy transfer assays. Org. Lett. 3 (2001) 1797-1800
23. Wang T., Pentyala S., Rebecchi M.J., and Scarlata S. Differential association of the pleckstrin homology domains of phospholipases C-β1, C-β2, and C-δ1 with lipid bilayers and the βγ subunits of heterotrimeric G proteins. Biochemistry 38 (1999) 1517-1524
24. Buck E., Schatz P., Scarlata S., and Iyengar R. Role of dynamic interactions in effective signal transfer for Gβ stimulation of phospholipase C-β2. J. Biol. Chem. 277 (2002) 49707-49715
25. Scarlata S. Determination of strength and specificity of membrane-bound G protein-phospholipase C association using fluorescence spectroscopy. Methods Enzymol. 345 (2002) 306-327
26. Tetin S.Y., Ruan Q., Saldana S.C., Pope M.R., Chen Y., Wu H., Pinkus M.S., Jiang J., and Richardson P.L. Interactions of two monoclonal antibodies with BNP: high resolution epitope mapping using fluorescence correlation spectroscopy. Biochemistry 45 (2006) 14155-14165
27. Muller J.D., Chen Y., and Gratton E. Resolving heterogeneity on the single molecular level with the photon-counting histogram. Biophys. J. 78 (2000) 474-486
28. Winder A.F., and Gent W.L. Correction of light-scattering errors in spectrophotometric protein determinations. Biopolymers 10 (1971) 1243-1251
29. Mach H., Middaugh C.R., and Lewis R.V. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal. Biochem. 200 (1992) 74-80
30. Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
31. Sillen A., and Engelborghs Y. The correct use of "average" fluorescence parameters. Photochem. Photobiol. 67 (1998) 457-468
32. Bevington P.R., and Robinson D.K. Data Reduction and Error Analysis for the Physical Sciences (1992), McGraw-Hill, New York
33. Rye H.S. Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction. Methods 24 (2001) 278-288