期刊
JOURNAL OF MOLECULAR STRUCTURE
卷 968, 期 1-3, 页码 24-31出版社
ELSEVIER
DOI: 10.1016/j.molstruc.2010.01.015
关键词
Coomassie brilliant blue G250; Human serum albumin; Binding mechanism; Binding site; Spectroscopic method; Molecular modeling
资金
- National Natural Science Foundation of China [20873096, 20921062]
- Key Laboratory of Catalysis and Materials Science of Hubei Province [CHCL09007]
- Hubei Provincial Education Department [D20092803]
- Ministry of Science and Technology of the People's Republic of China [2009CB939705]
The interaction between coomassie brilliant blue G250 and human serum albumin was investigated by spectroscopic methods such as fluorescence quenching, synchronous fluorescence, 3D fluorescence spectra, circular dichroism spectra and UV-vis absorption as well as molecular modeling. The fluorescence quenching of human serum albumin by coomassie brilliant blue G250 was attributed to static interaction. The binding reaction was mainly enthalpy-driven. Both van der Waals and hydrogen bonding forces played major roles in stabilizing the coomassie brilliant blue G250-human serum albumin complex. The Stern-Volmer quenching constant (K-SV) and corresponding thermodynamic parameters (Delta H-circle minus, Delta G(circle minus) and Delta S-circle minus) were determined. Site marker competitive experiments indicated that coomassie brilliant blue G250 bound to site I (subdomain IIA) of human serum albumin. Molecular docking study further confirmed the binding mode obtained by experimental study. The conformational investigation demonstrated very minor micro-environmental and conformational changes in human serum albumin molecules. (C) 2010 Elsevier B.V. All rights reserved.
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