【摘要】 运用密度泛函理论B3LYP/6-31G*方法对缬沙坦的几何构型进行了全优化和前线轨道分析;用荧光光谱法研究了标题化合物与牛血红蛋白(BHB)的相互作用,实验结果表明它们的结合位点数n约为1,结合常数K为759.94 L.mol-1;用分子柔性对接技术确定了它们之间的作用位点、作用力类型及相互作用能,结果显示标题化合物与BHB中C链上的Thr 39形成氢键,相互作用静电能是-280.3 kcal/mol,范德华力为-190.0 kcal/mol,势能为-319.6 kcal/mol.更多还原

【Abstract】 The structures of valsartan were optimized in the ground state using B3LYP/6-31G* methods.The interaction between valsartan and bovine hemoglobin(BHB) was investigated using flexible fluorescence and molecule docking technology.Experimental results showed that the binding site number n was about 1,and the co-apparent binding constant KA was 759.94 L·mol-1.Molecular modeling was carried out to investigate the interaction site,interaction styles and the interaction energy.A hydrogen bond was formed between valsartan and Thr39 in the C chains of BHB.The values of electrostatic energy,van der waals energy and potential energy were-280.3kcal/mol,-190.0kcal/mol,and-319.6kcal/mol respectively.更多还原