分子对接模拟与光谱法研究没食子酸丙酯和牛血清白蛋白的相互作用
Study on the interaction between propyl gallate and bovine serum albumin using fluorescence spectroscopy and molecular docking
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摘要: 运用荧光光谱法、紫外吸收光谱法等方法对没食子酸丙酯（PG）与牛血清白蛋白（BSA）之间的相互作用进行了研究。荧光猝灭计算结果表明PG与BSA间的结合作用较强,猝灭机制为静态猝灭,测得其299 K时的结合常数KA为1.03×105L·mol-1,两者的作用距离为1.71 nm。热力学参数计算结果表明PG与BSA相互作用力主要为范德华力与氢键作用力。通过探针分子取代反应确定了PG在BSA上的结合位点是亚级结构域IIA。圆二色谱的测定结果表明PG的结合导致了蛋白中α-螺旋结构的减少以及无规则卷曲的增加。本文最后通过计算机模拟分子Dock的方法模拟出了PG与BSA的结合构象,所得到的结合参数与之前的计算结果相符。Abstract: The interaction between propyl gallate( PG) and BSA was studied by the spectroscopy method in vitro.The quenching mechanism was a static quenching procedure,and the binding constants KAbetween PG and BSA was obtained to be 1.03 × 105L·mol- 1while the binding distance was calculated as 2.2 nm at 299 K. The thermodynamic calculations suggested the van der Waals interactions and the hydrogen bonds play a major part in the interaction between BSA and PG.The further study of binding site showed there was one PG- binding site in the subdomain IIA of BSA. CD spectroscopic further showed that drug complexation altered protein conformation by a major reduction of α- helix inducing a partial protein destabilization. In addition,the result of autodocking for PG and BSA was simulated,and the parameters of the binding were accorded with the results of the calculation.
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