荧光光谱法研究山姜素与牛血清白蛋白的相互作用机理

Study on the Interaction Mechanism of Alpinetin with Bovine Serum Albumin by Fluorescence Spectroscopy

研究了模拟生理条件下,山姜素与牛血清白蛋白(BSA)的相互作用。山姜素猝灭BSA为静态猝灭过程,获得了不同温度下山姜素与BSA的结合常数和结合位点数。考察了Mg2+、Ca2+、Zn2+、Cu2+等金属离子对结合作用的影响。热力学参数研究发现静电作用力为山姜素与BSA的主要结合力。根据Frster非辐射能量转移理论,计算了山姜素与BSA之间的结合距离r0为4.07nm。同步荧光光谱法研究结果表明山姜素对酪氨酸残基的微环境产生了影响,使其疏水性增强,而对色氨酸残基的微环境没有产生影响。

The interaction between alpinetin and bovine serum albumin(BSA)was studied under simulated physiological conditions.Alpinetin quenches the fluorescence of BSA via a static quenching process.The binding affinity and number of binding sites were measured at different temperatures.Effects of Mg2+,Ca2+,Zn2+and Cu2+on the binding were also studied.Thermodynamic parameters obtained revealed that electrostatic interaction is the primary force between alpinetin and BSA.According to Frster′s non-radiative energy transfer theory,the distance r0 between alpinetin and BSA found was calculated to be 4.07 nm.The synchronous fluorescence spectra showed the vicinity of tyrosine residue become more hydrophobicity,which no effect was found surrounding the tryptophan residue.