5-硝基-1H-吲哚-2-羧酸与牛血红蛋白相互作用的分子模拟与光谱研究  

Molecule simulation and spectroscopic studies of interaction between 5-nitro-1H-indole-2-acid and bovine hemoglobin

作　　者：毛慧[1] 蔡炳锋[1] 赵波[1] 李利[1] 沈健[1] 

机构地区：[1]江苏省生物功能材料重点实验室,南京师范大学化学与环境科学学院,江苏南京210097

出　　处：《化学研究与应用》2009年第5期675-679,共5页Chemical Research and Application

基　　金：国家高技术研究发展计划(863计划)(2006AA03Z445)资助项目;江苏高校自然科学基金(07KJD150098)资助项目;江苏省科技厅自然科学基金(BK2008372)资助项目

摘　　要：运用密度泛函理论B3LYP/6-31G*方法对5-硝基-1H-吲哚-2-羧酸(NIA)的几何构型进行了全优化。在这基础上,用分子对接技术确定了NIA与牛血红蛋白(BHb)之间的作用位点、作用力类型及相互作用能。理论计算的结果表明NIA和BHb相互作用的静电能是-208.9 kcal.mol-1,范德华能为-180.5 kcal.mol-1,势能为-389.4 kcal.mol-1。NIA与BHb中A链上的Leu129、Ser133残基形成氢键,而NIA分子中的骨架苯环部分易与疏水氨基酸,包括产生荧光的Tyr残基等发生作用,这与NIA能使BHb荧光淬灭的实验结果是一致的。The geometrical structure of 5-nitro-1H-indole-2-acid （NIA） was optimized at the B3 LYP/6-31G＊ level. Based on this structure,the position, type and energy of the interaction between NIA and bovine hemoglobin （BHb）was investigated using the molecule docking technology. It was obtained from the theoretical calculation that the values of electrostatic energy, van der waals energy and potential energy of the interaction between NIA and BHb are -208.9,-180.5 and -389.4 kcal·mol^-1 ,respectively. The hydrogen bonds of NIA with Leu129,Ser133 in the A chain of BHb is formed. The framework of the benzene ring in NIA is easy to interact with the hydrophobic amino acid residues, including Tyr residue, which can produce fluorescence. It leads to the fluorescence quenching of BHb. This is in good agreement with the result of the fluorescence experiments. In addition, electronic absorption spectrum of NIA calculated with the time-dependent density functional theory （TD-DFT）is similar to the UV absorption spectrum of NIA obtained from the experiment.

关 键 词：5-硝基-1H-吲哚-2-羧酸 牛血红蛋白 相互作用 分子模拟 

分 类 号：O641[理学—物理化学]