Spectroscopic probe analysis for exploring probe-protein interaction: A mapping of native, unfolding and refolding of protein bovine serum albumin by extrinsic fluorescence probe

Biophysical Chemistry

Volumn 156, Issue 2-3, 2011, Pages 128-139

  Samanta, Anuva ^a   Paul, Bijan Kumar ^a   Guchhait, Nikhil ^a  

^a UNIVERSITY OF CALCUTTA   (India)

Author keywords

benzaldehyde; Bovine serum albumin; Circular dichroism; Denaturant; Energy transfer; Fluorescence spectroscopy; para N,N dimethylamino orthohydroxy

Indexed keywords

4 N,N DIMETHYLAMINO 2 HYDROXYBENZALDEHYDE; ACRYLAMIDE; BOVINE SERUM ALBUMIN; FLUORESCENT DYE; UNCLASSIFIED DRUG;

ALPHA HELIX; ANISOTROPY; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; COMPLEX FORMATION; CONCENTRATION RESPONSE; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MEASUREMENT; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN UNFOLDING; STEADY STATE;

AMINOPHENOLS; ANIMALS; BENZALDEHYDES; CATTLE; CIRCULAR DICHROISM; FLUORESCENT DYES; PROTEIN BINDING; PROTEIN REFOLDING; PROTEIN UNFOLDING; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS;

BOVINAE;

EID: 79956096387     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.03.008     Document Type: Article

References (52)

1. D.C. Carter, J.X. Ho, Structure of serum albumin, Adv. Protein Chem. 45 (1994) 153-203.
2. Y. Moriyama, D. Ohta, K. Hadiya, Y. Mitsui, K. Takeda, Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins, J. Protein Chem. 15 (1996) 265-272. (Pubitemid 26179086)
3. J.K. Choi, J. Ho, S. Curry, D. Qin, R. Bittman, J.A. Hamilton, Interactions of very long-chain saturated fatty acids with serum albumin, J. Lipid Res. 43 (2002) 1000-1010. (Pubitemid 34760870)
4. S. Makino, J.A. Reynolds, C. Tanford, The binding of deoxycholate and Triton X-100 to proteins, J. Biol. Chem. 248 (1973) 4926-4932.
5. Y. Zhang, D.E. Wilcox, Thermodynamic and spectroscopic study of CuII and NiII binding to bovine serum albumin, J. Biol. Inorg. Chem. 7 (2002) 327-337. (Pubitemid 36056385)
6. K. Kamikubo, S. Sakata, S. Nakamura, T. Komaki, K. Miura, Thyroxine binding to human serum albumin immobilized on sepharose and effects of nonprotein albumin-binding plasma constituents, J. Protein Chem. 9 (1990) 461-465. (Pubitemid 20308945)
7. B. Sengupta, P.K. Sengupta, The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study, Biochem. Bioph. Res. Co. 299 (2002) 400-403. (Pubitemid 35365642)
8. X.Z. Feng, Z. Liu, L.J. Yang, C. Wang, C.L. Bai, Investigation of the interaction between acridine orange and bovine serum albumin, Talanta 47 (1998) 1223-1229.
9. S. Chatterjee, T.S. Srivastava, Spectral investigations of the interaction of some porphyrins with bovine serum albumin, J. Porphyr. Phthalocya. 4 (2000) 147-157.
10. Y.J. Hu, Y. Liu, J.B. Wang, et al., Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin, J. Pharmaceut. Biomed. 36 (2004) 915-919.
11. Y.Q. Wang, H.M. Zang, G.C. Zang, et al., Interaction of the flavonoid hesperidin with bovine serum albumin: a fluorescence quenching study, J. Pharmaceut. Biomed. 43 (2007) 1869-1875.
12. T. Peters, Serum albumin, Adv. Protein Chem. 37 (1985) 161-245.
13. J.F. Foster, Albumin Structure, Function and Uses; Pergamon Press, Oxford, UK, 1977.
14. A. Papadopoulou, R.J. Green, R.A. Frazier, Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study, J. Agr. Food Chem. 53 (2005) 158-163.
15. V. Daggett, A. Fersht, The present view of the mechanism of protein folding, Nat. Rev. Mol. Cell Bio. 4 (2003) 497-502. (Pubitemid 36648595)
16. G. Taubes, Misfolding the way to dise, Science 271 (1996) 1493-1495.
17. C.M. Dobson, Principles of protein folding, misfolding and aggregation, Semin. Cell Dev. Biol. 15 (2004) 3-16.
18. E.D. Goddard, Interaction of surfactant with polymers and proteins, Protein-Surfactant Interactions, CRC Press, Boca Raton, New York, 1993.
19. C. Tanford, The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd ed Wiley-Interscience, New York, 1980.
20. S. Shingawa, M. Sato, K. Kameyama, T. Takagi, Effect of salt concentration on the structure of protein-sodium dodecyl sulfate complexes revealed by small-angle X-ray scattering, Langmuir 10 (1994) 1690-1694.
21. J. Oakes, Protein-surfactant interactions. Nuclear magnetic resonance and binding isotherm studies of interactions between bovine serum albumin and sodium dodecyl sulphate, J. Chem. Soc., Faraday Trans. 1 70 (1974) 2200-2209.
22. N.J. Turro, X.-G. Lei, K.P. Ananthapadmanabhan, M. Aronson, Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system, Langmuir 11 (1995) 2525-2533.
23. X.H. Guo, N.M. Zhao, S.H. Chen, J. Teixeira, Small-angle neutron scattering study of the structure of protein/detergent complexes, Biopolymers 29 (1990) 335-346. (Pubitemid 20079197)
24. M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
25. O.H. Lowry, N.J. Rosebrough, A.L. Farr, R.J. Randall, Protein measurement with the folin-phenol reagents, J. Biol. Chem. 193 (1951) 265-275.
26. F. Joseph, The biuret method of estimating albumin and globulin in serum and urine, Biochem. J. 29 (1935) 799-803.
27. G.M. Edelman, W.O. Mcclure, Fluorescent probes and the conformation of proteins, Acc. Chem. Res. 1 (1968) 65-70.
28. L. Brand, J.R. Gohlke, Fluorescence probes for structure, Annu. Rev. Biochem. 41 (1972) 843-868.
29. A.P. Demchenko, Topics in Fluorescence Spectroscopy: Biochemical Applications, Plenum, New York, 1992.
30. R.B. Singh, S. Mahanta, A. Bagchi, N. Guchhait, Interaction of human serum albumin with charge transfer probe ethyl ester of N, N-dimethylamino naphthyl acrylic acid: an extrinsic fluorescence probe for studying protein microenvironment, Photochem. Photobiol. Sci. 8 (2009) 101-110.
31. R.B. Singh, S. Mahanta, N. Guchhait, Destructive and protective action of sodium dodecyl sulphate micelles on the native conformation of bovine serum albumin: a study by extrinsic fluorescence probe 1-hydroxy-2-naphthaldehyde, Chem. Phys. Lett. 463 (2008) 183-188.
32. S. Mahanta, R.B. Singh, N. Guchhait, Study of proteinâ€''probe interaction and protective action of surfactant sodium dodecyl sulphate in urea-denatured HSA using charge transfer fluorescence probe methyl ester of N, N-dimethylamino naphthyl acrylic acid, J. Fluoresc. 19 (2009) 291-302.
33. S. Ghosh, N. Guchhait, Chemically induced unfolding of bovine serum albumin by urea and sodium dodecyl sulfate: a spectral study with the polarity-sensitive charge-transfer fluorescent probe (E)-3-(4-methylaminophenyl) acrylic acid methyl ester, Chem. Phys. Chem. 10 (2009) 1664-1671.
34. B.K. Paul, A. Samanta, N. Guchhait, Exploring hydrophobic subdomain iia of the protein bovine serum albumin in the native, intermediate, unfolded, and refolded states by a small fluorescence molecular reporter, J. Phys. Chem. B 114 (2010) 6183-6196.
35. A. Mallick, B. Halder, N. Chattopadhyay, Spectroscopic investigation on the interaction of ICT probe 3-acetyl-4-oxo-6,7-dihydro-12H Indolo-[2,3-a] quinolizine with serum albumins, J. Phys. Chem. B 109 (2005) 14683-14690.
36. S. Mahanta, R.B. Singh, S. Kar, N. Guchhait, Evidence of coupled photoinduced proton transfer and intramolecular charge transfer reaction in para-N, N-dimethylamino orthohydroxy benzaldehyde: spectroscopic and theoretical studies, Chem. Phys. 354 (2008) 118-129.
37. M. Fischer, J. Georges, Fluorescence quantum yield of rhodamine 6G in ethanol as a function of concentration using thermal lens spectrometry, Chem. Phys. Lett. 260 (1996) 115-118.
38. P. Mandal, S. Kundu, T. Misra, S.K. Roy, T. Ganguly, Effects of liquid crystal environment on the spectroscopic and photophysical properties of well-known reacting systems 2,3-dimethylindole (DMI) and 9-cyanoanthracene (9CNA), J. Phys. Chem. A 111 (2007) 11480-11486. (Pubitemid 350197591)
39. S. Dahne, W. Freyer, K. Teuchner, J. Dobkowski, Z.R. Grabowski, Dual and multiple fluorescence mechanisms of p-dimethylaminobenzaldehyde and its trimethylene-bridged double molecule, J. Lumin. 22 (1980) 37-49. (Pubitemid 12423700)
40. J. Catalan, F. Toriblo, A.U. Acuna, Intramolecular hydrogen bonding and fluorescence of salicylaldehyde, salicylamide, and o-hydroxyacetophenone in gas and condensed phase, J. Phys. Chem. 86 (1982) 303-306.
41. A. Samanta, B.K. Paul, S. Mahanta, R.B. Singh, S. Kar, N. Guchhait, Evidence of acid mediated enhancement of photoinduced charge transfer reaction in 2-methoxy-4-(N, N-dimethylamino)benzaldehyde: spectroscopic and quantum chemical study, J. Photochem. Photobiol. A Chem. 212 (2010) 161-169.
42. A. Chattopadhyay, S. Mukherjee, Fluorophore environments in membrane-bound probes: a red edge excitation shift study, Biochemistry 32 (1993) 3804-3811. (Pubitemid 23126960)
43. J.R. Lackowicz, Principles of Fluorescence Spectroscopy, 3rd ed. Plenum Press, New York, 2006.
44. R.E. Maurice, A.G. Camillo, Fluorescence quenching studies with proteins, Anal, Biochem. 114 (1981) 199-212.
45. S.S. Lehrer, Solute perturbation of protein fluorescence quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion, Biochemistry 10 (1971) 3254-3263.
46. P.D. Ross, S. Subramanian, Thermodynamics of protein association reactions: forces contributing to stability, Biochemistry 20 (1981) 3096-3102.
47. T. Förster, Transfer mechanisms of electronic excitation, Discuss. Faraday Soc. 27 (1959) 7-17.
48. J.B.F. Lloyd, Synchronized excitation of fluorescence emission spectra, Nature 231 (1971) 64-65.
49. N.L. Vekshin, Separation of the tyrosine and tryptophan components of fluorescence using synchronous scanning method, Biofizika 41 (1996) 1176-1179.
50. J. Kang, Y. Liu, M.X. Xie, S. Li, M. Jiang, Y.D. Wang, Interactions of human serum albumin with chlorogenic acid and ferulic acid, Biochim. Biophys. Acta 1674 (2004) 205-212.
51. P. Yang, F. Gao, The Principle of Bioinorganic Chemistry, Science Press, 2002.
52. N. Greenfield, G.D. Fasman, Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8 (1969) 4108-4116.