中文摘要：

HIV-1蛋白酶是治疗艾滋病的重要靶标酶之一.采用分子动力学模拟,运用MM-PBSA方法计算了HIV-1蛋白酶与三个抑制剂BE4,BE5和BE6的结合自由能,结果表明抑制剂P1/P11位置的苄基上双氟原子的不同位置对结合自由能产生不同的影响.通过能量分解的方法考察了HIV-1蛋白酶的主要残基与三个抑制剂间的相互作用与识别,结果表明三个抑制剂以相同的作用模式与HIV-1蛋白酶结合,计算结果与实验结果基本吻合.

英文摘要：

HIV-1 protease is an important target of AIDS chemotherapy.Molecular dynamics simulations followed by MM-PBSA analyses were performed to study the binding of inhibitors BE4,BE5 and BE6 to HIV-1 protease.The results show that positioning of the fluorine atoms on the benzyloxy group of P1/P11 of the inhibitors affects their binding free energies.Inhibitor-residue interactions calculated provide some insights into the mechanisms of enzyme-inhibitor binding.Our results indicate that the three inhibitors bind to HIV-1 protease in a very similar mode.The calculated data agree well with experimental findings.