荧光和紫外光谱法研究柯里拉京与人血清白蛋白之间的相互作用

Study on Interaction of Corilagin and HSA by Fluorescence and UV Spectroscopies

在模拟人体血液pH条件(pH 7.4,离子强度0.1mol·L-1),通过荧光猝灭、同步荧光、3D荧光和紫外吸收光谱等方法研究了柯里拉京(Cor)与人血清白蛋白(HSA)之间相互作用机制。结果表明:HSA的荧光能被Cor静态猝灭,两者间结合常数为2.79×103(298K),2.22×104(304K)和8.41×104 L·mol-1(310K)。根据Van’t Hoff方程结果显示,Cor与HSA间的作用主要为疏水作用,其作用过程为自发、吸热。基于Frster能量转移,得知Cor与HSA间结合距离为9.33nm。标记竞争实验指出,Cor优先结合HSA的位点Ⅲ。3D荧光光谱、同步荧光光谱和紫外吸收光谱显示,与Cor作用对HSA构象影响不显著。

Under the simulative physiological conditions(pH 7.4,ionic strength 0.1mol·L-1)the interaction between Corilagin(Cor)and human serum albumin(HSA)was investigated by fluorescence spectroscopy,synchronous fluorescence,3Dfluorescence and ultraviolet absorption spectra.Results showed that the main quenching mechanism between Cor and HSA was a static quenching process.All the magnitude binding constants(KA)were 2.79×103(298K),2.22×104(304K)and 8.41×104L·mol-1(310K).According to Van’t Hoff equation,the interaction between Cor and HSA was mainly hydrophobic interaction.The binding distances between Cor and HSA was 9.33 nm based on Frster energy transformation.It was pointed out by marker competition experiments that the primary binding site for Cor was located at siteⅢin the HSA.3Ddimensional,synchronous fluorescence spectrum and ultraviolet absorption spectra showed that the conformation of HSA did not change apparently with the addition of Cor.