[Spectroscopic study on the interaction between resveratrol and human serum albumin].
The interaction between resveratrol and human serum albumin (HSA) was studied by using fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet spectra. The Stern-Volmer curve of the fluorescence quenching of HSA by resveratrol indicated that the quenching mechanism between resveratrol and HSA was mainly static quenching, with nonradiation energy transfer occurring within single molecule. The binding constants (KA) were 2.39 x 10(5) (25 degrees C), 1.25 x 10(5) (35 degrees C) and 1.10 x 10(5) (45 degrees C), respectively. According to the Forster theory of nonradiation energy transfer, the binding distances (r) were 3.02 nm (25 degrees C), 3.46 nm (35 degrees C) and 3.79 nm (45 degrees C), respectively. The thermodynamic parameters showed that the interaction between resveratrol and HSA was mainly driven by hydrophobic force. Synchronous spectrum was used to investigate the conformational change of HSA.
Wu
Qiu-Hua
QH
Key Laboratory of Bioinorganic Chemistry, College of Science, Agricultural University of Hebei, Baoding 071001, China.
Zhou
Xin
X
Zang
Xiao-Huan
XH
Wang
Chun
C
Zhang
Zhi-Heng
ZH
Wang
Zhi
Z
D020533:Angiogenesis Inhibitors; D006801:Humans; D007109:Immunity / Q000187:drug effects* / Q000276:immunology; D000077185:Resveratrol; D012709:Serum Albumin / Q000187:drug effects* / Q000276:immunology; D013057:Spectrum Analysis; D013267:Stilbenes / Q000494:pharmacology*
D020533:Angiogenesis Inhibitors; D012709:Serum Albumin; D013267:Stilbenes; D000077185:Resveratrol