title: [Interaction of quercetin and bovine serum albumin].
abstract: The interaction of quercetin and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The apparent binding constants (KA) between quercetin and BSA were 2.8 x 10(8) (26 degrees C) and 3.1 x 10(8) (36 degrees C), and the binding sites (n) were 1.7+/-0.02. According to the Förster theory of non-radiation energy transfer, the binding distances (r) were also obtained. The experimental results showed that the quercetin could be inserted into the BSA, quenching the inner fluorescence by forming the quercetin-BSA complex. It was found that both static quenching and non-radiation energy transfer were the main reasons for the fluorescence quenching. The process of binding was a spontaneous molecular interactioln in which entropy increased while Gibbs free energy decreased, indicating that the interaction of quercetin and BSA was driven mainly by hydrophobic force.
authors.affiliation: College of Sciences, Agricultural University of Hebei, Baoding 071001, China.
authors.forename: Chun
authors.initials: C
authors.lastname: Wang
authors.forename: Qiu-Hua
authors.initials: QH
authors.lastname: Wu
authors.forename: Zhi
authors.initials: Z
authors.lastname: Wang
authors.forename: Da-Gang
authors.initials: DG
authors.lastname: Chen
mesh_terms: D000465:Algorithms; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D005453:Fluorescence; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D011485:Protein Binding; D011794:Quercetin / Q000737:chemistry* / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine; D011794:Quercetin