Binding stoichiometry and affinity of fluorescent dyes to proteins in different structural states

Methods in Molecular Biology

Volumn 895, Issue , 2012, Pages 441-460

  Sulatskaya, Anna I ^a   Povarova, Olga I ^a   Kuznetsova, Irina M ^a   Uversky, Vladimir N ^b,c   Turoverov, Konstantin K ^a  

^a INSTITUTE OF CYTOLOGY   (Russian Federation)

^b UNIVERSITY OF SOUTH FLORIDA   (United States)

^c INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

Author keywords

ANS; Binding affinity; Binding stoichiometry; Bovine serum albumin; Equilibrium microdialysis; Fluorescence intensity; Fluorescence quantum yield; Fluorescent dyes

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; 8-ANILINO-1-NAPHTHALENESULFONIC ACID; BOVINE SERUM ALBUMIN; FLUORESCENT DYE;

ALGORITHM; ANIMAL; ARTICLE; CATTLE; CHEMISTRY; FLUORESCENCE; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY;

ALGORITHMS; ANILINO NAPHTHALENESULFONATES; ANIMALS; CATTLE; FLUORESCENCE; FLUORESCENT DYES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE;

EID: 84865340651     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-927-3_26     Document Type: Article

References (44)

1. Stryer L (1965)The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. JMol Biol 13:482-495
2. Peters T Jr (1996) All about albumin: biochemistry, genetics, and medical application. Academic Press, NewYork
3. LeVine H III (1993) Thioflavine T interaction with synthetic Alzheimer's disease betaamyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2:404-410
4. Levine H III (1995) Soluble multimeric Alzheimer beta(1-40) pre-amyloid complexes in dilute solution. Neurobiol Aging 16:755-764
5. Groenning M (2009) Binding mode of thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J Chem Biol 3:1-18
6. Voropay ES, Samtsov MP, Kaplevsky KN, Maskevich AA, Stepuro VI, Povarova OI, Kuznetsova IM, Turoverov KK, Fink AL, Uversky VN (2003) Spectral properties of thioflavin T and its complexes with amyloid fibrils. J Appl Spectrosc 70:868-874
7. Maskevich AA, Stsiapura VI, Kuzmitsky VA, Kuznetsova IM, Povarova OI, Uversky VN, Turoverov KK (2007) Spectral properties of thioflavin T in solvents with different dielectric properties and in a fibril-incorporated form. J Proteome Res 6:1392-1401
8. Sulatskaya AI, Kuznetsova IM, Maskevich AA, Uversky VN, Turoverov KK (2010) Nonradiative deactivation of the excited state of thioflavin T: dependence on solvent viscosity and temperature. PLoS One 5:e15385
9. Daughdrill GW, Pielak GJ, Uversky VN, Cortese MS, Dunker AK (2004) Natively disordered proteins, vol I. Wiley-VCH Verlag GmbH & Co, Weinheim, pp 271-353
10. Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, Gilmanshin RI (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31:119-128
11. Semisotnov GV, Rodionova NA, Kutyshenko VP, Ebert B, Blanck J, Ptitsyn OB (1987) Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett 224:9-13
12. Goto Y, Fink AL (1989) Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry 28:945-952
13. Rodionova NA, Semisotnov GV, Kutyshenko VP, Uverskii VN, Bolotina IA (1989) Staged equilibrium of carbonic anhydrase unfolding in strong denaturants. Mol Biol (Mosk) 23:683-692
14. Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI (1990) Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett 262:20-24
15. Ptitsyn OB (1995) Molten globule and protein folding. Adv Protein Chem 47:83-229
16. Povarova OI, Kuznetsova IM, Turoverov KK (2010) Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates. PLoS One 5:e15035
17. Dolgikh DA, Gilmanshin RI, Brazhnikov EV, Bychkova VE, Semisotnov GV, Venyaminov S, Ptitsyn OB (1981) Alpha-lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett 136:311-315
18. Uversky VN, Li, J, Fink AL (2001) Evidence for a partially-folded intermediate in a-synuclein fibrillation. J BiolChem276(14):10737-10744
19. Uversky VN, Ptitsyn OB (1996) All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Fold Des 1:117-122
20. Uversky VN, Winter S, Lober G (1998) Selfassociation of 8-anilino-1-naphthalene-sulfonate molecules: spectroscopic characterization and application to the investigation of protein folding. Biochim Biophys Acta 1388:133-142
21. Klimtchuk E, Venyaminov S, Kurian E, Wessels W, Kirk W, Prendergast FG (2007) Photophysics of ANS. I. Protein-ANS complexes: intestinal fatty acid binding protein and single-trp mutants. Biophys Chem 125:1-12
22. Kirk W (2007) Photophysics of ANS. II: charge transfer character of near-UV absorption and consequences for ANS spectroscopy. Biophys Chem 125:13-23
23. Kirk W, Klimtchuk E (2007) Photophysics of ANS. III: circular dichroism of ANS and anilinonaphthalene in I-FABP. Biophys Chem 125:24-31
24. Kirk W, Wessels W (2007) Photophysics of ANS. IV. Electron transfer quenching of ANS in alcoholic solvents and mixtures. Biophys Chem 125:32-49
25. Kirk W, Kurian E, Wessels W (2007) Photophysics of ANS. V. Decay modes of ANS in proteins: the IFABP-ANS complex. Biophys Chem 125:50-58
26. Hawe A, Sutter M, Jiskoot W (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25:1487-1499
27. Neyroz P, Zambelli B, Ciurli S (2006) Intrinsically disordered structure of Bacillus pasteurii UreG as revealed by steady-state and timeresolved fluorescence spectroscopy. Biochemistry 45:8918-8930
28. Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD (2001) Clusterin, a binding protein with a molten globule-like region. Biochemistry 40:11828-11840
29. Lavery DN, McEwan IJ (2008) Structural characterization of the native NH2-terminal transactivation domain of the human androgen receptor: a collapsed disordered conformation underlies structural plasticity and proteininduced folding. Biochemistry 47:3360-3369
30. Humphreys DT, Carver JA, Easterbrook-Smith SB, WilsonMR(1999)Clusterin has chaperonelike activity similar to that of small heat shock proteins. J Biol Chem 274:6875-6881
31. Wilson MR, Easterbrook-Smith SB (2000) Clusterin is a secreted mammalian chaperone. Trends Biochem Sci 25:95-98
32. Calero M, Tokuda T, Rostagno A, Kumar A, Zlokovic B, Frangione B, Ghiso J (1999) Functional and structural properties of lipidassociated apolipoprotein J (clusterin). Biochem J 344(Pt 2):375-383
33. Bailey R, Griswold MD (1999) Clusterin in the male reproductive system: localization and possible function. Mol Cell Endocrinol 151:17-23
34. Lavery DN, McEwan IJ (2005) Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations. Biochem J 391:449-464
35. Uversky VN, Winter S, Lober G (1996) Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state. Biophys Chem 60:79-88
36. Eftink MR, Ghiron CA (1976) Fluorescence quenching of indole and model micelle systems. J Phys Chem 80:486-493
37. Roberts LM, Dunker AK (1993) Structural changes accompanying chloroform-induced contraction of the filamentous phage fd. Biochemistry 32:10479-10488
38. Turoverov KK, Kuznetsova IM, Maskevich AA, Stepuro VI, Kuzmitsky VA, Uversky VN (2007) Tht as an instrument for testing and investigation of amyloid and amyloid-like fibrils. Proc SPIE 6733:1-7
39. Sulatskaya AI, Kuznetsova IM, Turoverov KK (2011) Interaction of thioflavin T with amyloid fibrils: stoichiometry and affinity of dye binding, absorption spectra of bound dye. J Phys Chem B 115:11519-11524
40. Sulatskaya AI, Kuznetsova IM, Turoverov KK (2012) Interaction of thioflavin T with amyloid fibrils: fluorescence quantum yield of bound dye. J Phys Chem B 116(8):2538-2544
41. Kuznetsova IM, Sulatskaya AI, Uversky VN and Turoverov KK (2012) Analyzing Thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique. Plos One 7(2): e30724
42. Turoverov KK, Biktashev AG, Dorofeiuk AV, Kuznetsova IM(1998) A complex of apparatus and programs for the measurement of spectral, polarization and kinetic characteristics of fluorescence in solution. Tsitologiia 40:806-817
43. Kurganov BI (2000) Analysis of negative cooperativity for glutamate dehydrogenase. Biophys Chem 87:185-199
44. DzwolakW, PeculM(2005) Chiral bias of amyloid fibrils revealed by the twisted confor-mation of thioflavin T: an induced circular dichroism/DFT study. FEBS Lett 579:6601-6603