中文摘要：

HIV-1蛋白酶（PR）是治疗艾滋病的重要靶标酶之一．笔者采用分子动力学模拟，运用MM—PBSA方法计算了PR与抑制剂BEB复合物的绝对结合自由能；运用能量分解的方法考察了PR的主要残基与BEB间的相互作用与识别，结果表明：残基GLY27、ALA28／ALA28＇,GLY49、ILE50／ILE50和ILE84／ILE84为PR与BEB的结合自由能提供了主要贡献．抑制剂BEB骨架上的OH基和NH基与残基ASP25／ASP25＇,ASP29和GLY27之间的氢键相互作用有利于复合物的稳定．计算结果与实验值吻合较好．

英文摘要：

HIV - 1 protease has been an important target for AIDS chemotherapy. Molecular dynamics simulations followed by MM - PBSA analysis have been performed to study binding of the inhibitor BEB to HIV - 1 protease （PR）. Inhibitor -residue interaction is calculated to understand binding mechanics. The results show that the interactions of residue GLY27 ,ALA28/ALA28＇, GLY49 and ILE50/ILE50with BEB provide main contributions to binding free energy. The H - bonds between the - OH of inhibitor BEB and residues ASP25/ASP25, ASP29, and the H - bond between - NH of inhibitor BEB and residues GLY27 are advantageous to stabilize the complex. The calculated binding free energy agrees well with the experimental data.