title: [Spectroscopic study on the interaction between resveratrol and human serum albumin].
abstract: 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.
authors.affiliation: Key Laboratory of Bioinorganic Chemistry, College of Science, Agricultural University of Hebei, Baoding 071001, China.
authors.forename: Qiu-Hua
authors.initials: QH
authors.lastname: Wu
authors.forename: Xin
authors.initials: X
authors.lastname: Zhou
authors.forename: Xiao-Huan
authors.initials: XH
authors.lastname: Zang
authors.forename: Chun
authors.initials: C
authors.lastname: Wang
authors.forename: Zhi-Heng
authors.initials: ZH
authors.lastname: Zhang
authors.forename: Zhi
authors.initials: Z
authors.lastname: Wang
mesh_terms: 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*
chemical_list: D020533:Angiogenesis Inhibitors; D012709:Serum Albumin; D013267:Stilbenes; D000077185:Resveratrol