荧光光谱法研究黄芩苷与牛血清白蛋白的相互作用

Interaction Between Baicalin and Bovine Serum Albumin by Fluorescence Spectrometry

在pH为7.40的T ris-HC l缓冲体系中,采用荧光光谱技术研究了黄芩苷与牛血清白蛋白(BSA)的相互作用。随着温度升高,黄芩苷与牛血清白蛋白的猝灭常数逐渐增大,表明黄芩苷对BSA的荧光猝灭为动态猝灭过程,由结合过程的热力学参数ΔH=51.708 kJ.m o-l 1>0和ΔS=265.075J.m o-l 1.K-1>0,推断黄芩苷与BSA之间主要靠疏水作用力相结合,生成自由能变(ΔG)为负值,表明黄芩苷与BSA的作用过程是一个自发过程;应用同步荧光光谱考察了黄芩苷对BSA构象的影响。

The interaction between baicalin and bovine serum albumin（BSA） in Tris-HCl buffer（pH 7.4） was studied by fluorescence spectrometry.The quenching constants at different temperatures were obtained,and the quenching constants increased with the increasing of temperature,which indicated that the interaction between baicalin and BSA was a dynamic quenching process.The thermodynamic parameters,enthalpy change（ΔH） and entropy change（ΔS）,were calculated to be 51.708kJ·mol-10,and 265.075J·mol-1·K-10,respectively,which indicated that the interaction of baicalin with BSA was driven mainly by hydrophobic interaction.The process of binding was a spontaneous process in which Gibbs free energy change（ΔG） was negative.The effect of baicalin on the conformation of BSA was analyzed by synchronous fluorescence spectrometry.