乙氧基白屈菜红碱与人血清白蛋白的相互作用

The Interaction of Human Serum Albumin with Ethoxychelerythine

采用荧光光谱法研究了乙氧基白屈菜红碱(ECHE)与人血清白蛋白(HSA)相互作用的机制.在模拟人体生理条件下,根据二者相互作用的光谱学特征,采用Lineweaver-Burk双倒数方程和热力学方程计算了三个温度下ECHE与HAS的结合参数.结果表明:在290K,300K,310K时ECHE与人血清白蛋白的结合常数分别为1.595×105 L?mol-1,1.718×105 L?mol-1,1.680×105 L?mol-1;结合位点数分别为1±0.06;二者之间的主要作用力为静电作用力.研究表明ECHE与人血清白蛋白之间作用生成了无荧光效应的复合物,属静态猝灭.

Fluorescence spectrophotometry was employed to investigate the interaction of human serum albumin（HSA） with ethoxysaguinarine（ECHE）. According to Lineweaver-Burk equation and thermodynamic equation, the binding constants and binding sites at different temperatures for the interaction of HSA with ethoxysaguinarine were obtained. The binding constants at three temperatures were 1.595×105Lmol-1（290K）, 1.718×105L ？ mol-1（300K） and 1.680×105L ？ mol-1（310K） respectively. The binding-site was about 1±0.06. The intermolecular forces between them were electrostatic forces. It was shown that ECHE quenches the fluorescence of HAS by forming the ECHE-BSA complex. The quenching mechanism in the experiment was mainly attributed to static quenching.