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.
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 va...
出处
《南京晓庄学院学报》
2008年第6期19-22,共4页
Journal of Nanjing Xiaozhuang University
基金
中国药科大学青年教师科技基金(E0619)
国家自然科学基金(20676051)
上海市科委重大科技攻关项目(07DZ19508)资助
关键词
牛血红蛋白
缬沙坦
荧光光谱
分子模拟
valsartan
bovine hemoglobin
fluorescence spectra
molecular modeling
