[粉防己碱与牛血清白蛋白相互作用的研究]

[Study on the interaction between fangchinoline and bovine serum albumin].

作者信息

Wu Qiu-hua, Wang Chun, Wang Zhi, Ma Jing-jun, Zang Xiao-huan, Qin Na-xin

机构信息

College of Science, Agricultural University of Hebei, Baoding 071001, China.

出版信息

Guang Pu Xue Yu Guang Pu Fen Xi. 2007 Dec;27(12):2498-501.

PMID:18330294

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.

摘要

采用荧光猝灭光谱、同步荧光光谱和紫外光谱等方法，研究了不同温度下汉防己甲素与牛血清白蛋白的结合反应。结果表明，汉防己甲素对牛血清白蛋白的荧光具有较强的猝灭能力。汉防己甲素对牛血清白蛋白荧光猝灭的Stern-Volmer曲线表明，汉防己甲素对牛血清白蛋白的猝灭机制为静态猝灭。根据Förster非辐射能量转移理论，不同温度下的结合距离（r）分别为2.51 nm（27℃）、2.72 nm（37℃）和2.89 nm（47℃），结合常数（KA）分别为1.05×10⁵ L·mol⁻¹（27℃）、3.31×10⁵ L·mol⁻¹（37℃）和7.24×10⁵ L·mol⁻¹（47℃）。热力学参数表明，汉防己甲素与牛血清白蛋白的相互作用主要由疏水作用力驱动。采用同步光谱研究了牛血清白蛋白的构象变化。