紫外吸收光谱和荧光光谱法研究大黄酚与牛血清白蛋白相互作用机制

Study on the Mechanism of Interaction Between Chrysophanol and Bovine Serum Albumin by UV-Absorptiospectrometry and Fluorospectrometry

利用紫外吸收光谱和荧光光谱法研究中药小分子大黄酚与牛血清白蛋白在不同的外界环境下的相互作用机制。结果表明:在近中性、弱酸性、弱碱性条件下大黄酚与牛血清白蛋白的相互作用而引起的荧光猝灭均属静态猝灭。采用位点结合模型公式、热力学公式和福斯特Foster非辐射能量转移机理求解出每种酸度下的结合常数、结合位点数、作用力类型以及结合距离。试验还表明:微量金属离子和有机溶剂对结合常数有一定的影响。

Mechanism of the interaction between chrysophanol and bovine serum albumin （BSA） under different external circumstances was studied by UV-absorptiospectrometry and fluorospectrometry. It was found that fluorescence quenching of the interaction either in nearly neutral, weakly acidic or weakly alkaline medium was due to static quenching. The binding constants, number of binding sites, types of the binding force and binding distances were found by applying the equation of model of site-binding, thermodynamic equations, and Foster theory of transfer of non-radiation energy. It was also shown that the binding constants were affected by the presence of trace amounts of metal ions and of several organic solvents.