白藜芦醇与人血清白蛋白相互作用的光谱研究

Spectroscopic Study on the Interaction between Resveratrol and Human Serum Albumin

在不同温度下,用荧光猝灭光谱、同步荧光光谱和紫外-可见吸收光谱,研究了白藜芦醇与人血清白蛋白(HSA)相互作用的光谱学行为。根据不同温度下白藜芦醇对HSA的荧光猝灭作用,利用Stern-Volmer方程处理实验数据,结果表明白藜芦醇与HSA的结合常数KA为2.39×105(25℃),1.25×105(35℃)和1.10×105(45℃)。根据F rster非辐射能量转移理论,求出了白藜芦醇与HSA之间的结合距离为3.02 nm(25℃),3.46 nm(35℃)和3.79 nm(45℃)。实验表明静态猝灭和非辐射能量转移是导致白藜芦醇对HSA荧光猝灭的两大原因,通过计算热力学参数,可知该药物与人血清白蛋白的相互作用是一个吉布斯自由能降低的自发过程,且二者之间的主要作用力类型为疏水作用力。并采用同步荧光光谱探讨了白藜芦醇对HSA构象的影响。

The interaction between resveratrol and human serum albumin（HSA） was studied by using fluorescence quenching spectra,synchronous fluorescence spectra and ultra-violet spectra.The Stern-Volmer curve of the fluorescence quenching of HSA by resveratrol indicated that the quenching mechanism between resveratrol and HSA was mainly static quenching,with nonradiation energy transfer occurring within single molecule.The binding constants（KA） were 2.39×105（25 ℃）,1.25×105（35 ℃） and 1.10×105（45 ℃）,respectively.According to the Forster theory of nonradiation energy transfer,the binding distances（r） were 3.02 nm（25 ℃）,3.46 nm（35 ℃） and 3.79 nm（45 ℃）,respectively.The thermodynamic parameters showed that the interaction between resveratrol and HSA was mainly driven by hydrophobic force.Synchronous spectrum was used to investigate the conformational change of HSA.