摘要
利用分子力学和分子动力学模拟方法优化人类丁酰胆碱酯酶(BuChE)的晶体结构(PDB Code:1XLU),在此基础上用分子对接程序(Affinity)将其抑制剂利伐斯的明(rivastigmine)和抑制剂TV-3326分别与BuChE进行对接,获得其复合物结构的理论模型。通过配体与受体之间相互作用能和结构的分析给出了与抑制剂的具体结合方式,明确BuChE与抑制剂结合时起重要作用的氨基酸残基,为基于人类丁酰胆碱酯酶三维结构药物设计提供了参考信息。
The model of human butyrylcholinesterase（BuChE） was optimized by using Molecular mechanics and Molecular dynamics（PDB Code：1XLU）.Based on this model,the complex structures ofthe inhibitors with BuChE were obtained and investigated through ligand-receptor docking studies by means of Affinity.The binding pattern predicted by the affinity module reveals some important residues interacted with inhibitors,and provides a further refinement of the BuChE inhibitor binding interaction as a basis for new structure-based design efforts.
基金
高等学校博士学科点专项科研基金(20070183046)
