title: [Study on the interaction between fangchinoline and bovine serum albumin].
abstract: The binding reaction of fangchinoline with bovine serum albumin was studied at different temperatures by fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet spectra. It was shown that fangchinoline has a strong ability of quenching the fluorescence of BSA. The Stern-Volmer curve of the fluorescence quenching of BSA by fangchinoline indicated that the quenching mechanism of fangchinoline to BSA was a static quenching. According to the Förster theory of non-radiation energy transfer, the binding distances (r) at different temperature were 2.51 nm (27 degrees C), 2.72 nm (37 degrees C) and 2.89 nm (47 degrees C), respectively, while the binding constants (KA) were 1.05 x 10(5) L x mol(-1) (27 degrees C), 3.31x 10(5) L x mol(-1) (37 degrees C), and 7.24 x 10(5) L x mol(-1) (47 degrees C), respectively. The thermodynamic parameters showed that the interaction of fangchinoline and BSA was mainly driven by hydrophobic force. Synchronous spectrum was used to investigate the conformational changes of BSA.
authors.affiliation: College of Science, Agricultural University of Hebei, Baoding 071001, China.
authors.forename: Qiu-hua
authors.initials: QH
authors.lastname: Wu
authors.forename: Chun
authors.initials: C
authors.lastname: Wang
authors.forename: Zhi
authors.initials: Z
authors.lastname: Wang
authors.forename: Jing-jun
authors.initials: JJ
authors.lastname: Ma
authors.forename: Xiao-huan
authors.initials: XH
authors.lastname: Zang
authors.forename: Na-xin
authors.initials: NX
authors.lastname: Qin
mesh_terms: D000818:Animals; D044182:Benzylisoquinolines / Q000737:chemistry*; D002417:Cattle; D004735:Energy Transfer; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D044182:Benzylisoquinolines; D012710:Serum Albumin, Bovine; C060802:fangchinoline