Reevaluation of ans binding to human and bovine serum albumins: Key role of equilibrium microdialysis in ligand - receptor binding characterization

PLoS ONE

Volumn 7, Issue 7, 2012, Pages

  Kuznetsova, Irina M ^a,b   Sulatskaya, Anna I ^a   Povarova, Olga I ^a   Turoverov, Konstantin K ^a  

^a RUSSIAN ACADEMY OF SCIENCES   (Russian Federation)

^b PETER THE GREAT ST PETERSBURG POLYTECHNIC UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BOVINE SERUM ALBUMIN; DRUG TRANSPORTER; FLUORESCENT DYE; HUMAN SERUM ALBUMIN; LIGAND; PROTEIN; UNCLASSIFIED DRUG;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING AFFINITY; DRUG PROTEIN BINDING; DRUG TRANSPORT; EQUILIBRIUM MICRODIALYSIS; FLUORESCENCE; LIGAND BINDING; LIGHT ABSORPTION; MICRODIALYSIS; RECEPTOR BINDING; SPECTROPHOTOMETRY; STOICHIOMETRY;

ANILINO NAPHTHALENESULFONATES; ANIMALS; CATTLE; HUMANS; MICRODIALYSIS; PROTEIN BINDING; SERUM ALBUMIN, BOVINE;

BOVINAE;

EID: 84864045423     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040845     Document Type: Article

References (49)

1. Groenning M, (2009) Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J Chem Biol: DOI 10.1007/s12154-2009-0027-12155.
2. Oravcova J, Bohs B, Lindner W, (1996) Drug-protein binding sites. New trends in analytical and experimental methodology. J Chromatogr B Biomed Appl 677: 1-28.
3. Togashi DM, Ryder AG, (2008) A fluorescence analysis of ANS bound to bovine serum albumin: binding properties revisited by using energy transfer. J Fluoresc 18: 519-526.
4. Togashi DM, Ryder AG, (2010) Assessing protein-surface interactions with a series of multi-labeled BSA using fluorescence lifetime microscopy and Forster Energy Resonance Transfer. Biophys Chem 152: 55-64.
5. Jain TK, Varshney M, Maitra A, (1989) Structural Studies of Aerosol OT Reverse Micellar Aggregates by FT-IR Spectroscopy. J Phys Chem 93: 7409-7416.
6. Ivy MA, Gallagher LT, Ellington AD, Anslyn EV, (2012) Exploration of plasticizer and plastic explosive detection and differentiation with serum albumin cross-reactive arrays. Chemical Science 3: 1773-1779.
7. Hawe A, Sutter M, Jiskoot W, (2008) Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25: 1487-1499.
8. LeVine H, 3rd (1995) Thioflavine T interaction with amyloid-sheet structures. Amyloid: Int J Exp Clin Invest 2: 1-6.
9. Groenning M, Norrman M, Flink JM, van de Weert M, Bukrinsky JT, et al. (2007) Binding mode of Thioflavin T in insulin amyloid fibrils. J Struct Biol 159: 483-497.
10. Panjehshahin MR, Bowmer CJ, Yates MS, (1989) A pitfall in the use of double-reciprocal plots to estimate the intrinsic molar fluorescence of ligands bound to albumin. Biochem Pharmacol 38: 155-159.
11. Sen P, Fatima S, Ahmad B, Khan RH, (2009) Interactions of thioflavin T with serum albumins: spectroscopic analyses. Spectrochim Acta A Mol Biomol Spectrosc 74: 94-99.
12. Bagatolli LA, Kivatinitz SC, Fidelio GD, (1996) Interaction of small ligands with human serum albumin IIIA subdomain. How to determine the affinity constant using an easy steady state fluorescent method. J Pharm Sci 85: 1131-1132.
13. Naik DV, Paul WL, Schulman SG, (1975) Fluorometric determination of drug-protein association constants: binding of pamaquine by bovine serum albumin. J Pharm Sci 64: 1677-1680.
14. Kubarych CJ, Adams MM, Anslyn EV, (2010) Serum Albumins as Differential Receptors for the Discrimination of Fatty Acids and Oils. Organic Letters 12: 4780-4783.
15. Adams MM, Anslyn EV, (2009) Differential Sensing Using Proteins: Exploiting the Cross-Reactivity of Serum Albumin To Pattern Individual Terpenes and Terpenes in Perfume. Journal of the American Chemical Society 131: 17068-17069.
16. Morimoto K, Kawabata K, Kunii S, Hamano K, Saito T, et al. (2009) Characterization of type I collagen fibril formation using thioflavin T fluorescent dye. J Biochem 145: 677-684.
17. Weber G, (1952) Polarization of the fluorescence of macromolecules. II. Fluorescent conjugates of ovalbumin and bovine serum albumin. Biochem J 51: 155-167.
18. Slavik J, (1982) Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim Biophys Acta 694: 1-25.
19. Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, et al. (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31: 119-128.
20. 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.
21. Anufrieva EV, Nekrasova TN, Sheveleva TV, Krakovyak MG, (1994) [Structure and structural transformations of macromolecules water-soluble polymers and luminescence of magnesium salt of 8-anilinenaphthalene-1-sulfonic acid.] Vysokomol Soed 36 449-456.
22. Gasymov OK, Glasgow BJ, (2007) ANS fluorescence: potential to augment the identification of the external binding sites of proteins. Biochim Biophys Acta 1774: 403-411.
23. Schonbrunn E, Eschenburg S, Luger K, Kabsch W, Amrhein N, (2000) Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc Natl Acad Sci U S A 97: 6345-6349.
24. Cardamone M, Puri NK, (1992) Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem J 282 (Pt 2): 589-593.
25. Takehara K, Yuki K, Shirasawa M, Yamasaki S, Yamada S, (2009) Binding properties of hydrophobic molecules to human serum albumin studied by fluorescence titration. Anal Sci 25: 115-120.
26. Sudlow G, Birkett DJ, Wade DN, (1975) The characterization of two specific drug binding sites on human serum albumin. Mol Pharmacol 11: 824-832.
27. Peters T, (1996) All about albumin: biochemistry, genetics, and medical application New York: Academic Press. 432 p.
28. 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.
29. Konkoli Z, (2011) Safe uses of Hill's model: an exact comparison with the Adair-Klotz model. Theor Biol Med Model 8: 1-17.
30. Collini M, D'Alfonso L, Baldini G, (2000) New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Sci 9: 1968-1974.
31. Fan YX, Zhou JM, Kihara H, Tsou CL, (1998) Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies. Protein Sci 7: 2631-2641.
32. Naiki H, Higuchi K, Hosokawa M, Takeda T, (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 177: 244-249.
33. LeVine H, 3rd (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2: 404-410.
34. Voropay ES, Samtsov MP, Kaplevsky KN, Maskevich AA, Stepuro VI, et al. (2003) Spectral properties of Thioflavin T and its complexes with amyloid fibrils. J Appl Spectrosc 70: 868-874.
35. Sulatskaya AI, Kuznetsova IM, Turoverov KK, (2012) Interaction of tye{cyrillic}hioflavin T with amyloid fibril: fluorescence quantum yield of bound dye. J Phys Chem B 116: 2538-2544.
36. Sulatskaya AI, Kuznetsova IM, Turoverov KK, (2011) The interaction of tye{cyrillic}hioflavin T with amyloid fibril: stoichiometry and affinity of dye binding, absorption spectra of bound dye. J Phys Chem B 115: 11519-11524.
37. Dzwolak W, Pecul M, (2005) Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: an induced circular dichroism/DFT study. FEBS Lett 579: 6601-6603.
38. 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.
39. Uversky VN, Winter S, Lober G, (1998) Self-association of 8-anilino-1-naphthalene-sulfonate molecules: spectroscopic characterization and application to the investigation of protein folding. Biochim Biophys Acta 1388: 133-142.
40. Kurganov BI, (2000) Analysis of negative cooperativity for glutamate dehydrogenase. Biophys Chem 87: 185-199.
41. Lee AG, Rogers J, Wilton DC, Ghiggino KP, Phillips D, (1978) Spectroscopic resolution of drug binding sites in biological membranes. FEBS Lett 94: 171-174.
42. Weber G, Young LB, (1964) Fragmentation of Bovine Serum Albumin by Pepsin. I. the Origin of the Acid Expansion of the Albumin Molecule. J Biol Chem 239: 1415-1423.
43. Stryer L, (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J Mol Biol 13: 482-495.
44. Matulis D, Lovrien R, (1998) 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J 74: 422-429.
45. Ptitsyn OB, (1995) Molten globule and protein folding. Adv Protein Chem 47: 83-229.
46. Bismuto E, Gratton E, Lamb DC, (2001) Dynamics of ANS binding to tuna apomyoglobin measured with fluorescence correlation spectroscopy. Biophys J 81: 3510-3521.
47. Georgiou ME, Georgiou CA, Koupparis MA, (1999) Automated flow injection gradient technique for binding studies of micromolecules to proteins using potentiometric sensors: application to bovine serum albumin with anilinonaphthalenesulfonate probe and drugs. Anal Chem 71: 2541-2550.
48. Hazra P, Chakrabarty D, Chakraborty A, Sarkar N, (2004) Probing protein-surfactant interaction by steady state and time-resolved fluorescence spectroscopy. Biochem Biophys Res Commun 314: 543-549.
49. Suarez Varela A, Sandez Macho MI, Minones J, (1992) Spectrofluorimetric study of the binding of 1-anilinonaphthalene-8-sulfonate to bovine serum albumin. J Pharm Sci 81: 842-844.