采用分子动力学模拟和结合自由能计算研究了抑制剂APV与HIV-1蛋白酶的作用机制.研究结果表明范德瓦尔斯作用主控了APV与HIV-1蛋白酶的结合.采用基于残基的自由能分解方法计算了抑制剂-残基相互作用,结果表明9个残基Gly27、Ile32、Val47、Ile50、Ile84、Ala28’、Gly49’、Ile50’和Arg87’与APV产生了大于1.0 kcal/mol的强相互作用,而且证明CH-π,CH-O相互作用和极性作用是其结合的主要形式.期待该结果可以为以HIV-1蛋白酶为靶标的抗艾滋病药物设计提供理论上的指导. The mechanism of action of inhibitor APV and HIV-1 protease was studied by molecular dynamics simulation and binding free energy calculation.The results show that the effect of van der Waals on the binding of APV and HIV-1 protease is based on the freedom of residues Inhibitor-residue interactions were calculated by decomposition, and the results showed that nine residues Gly27, Ile32, Val47, Ile50, Ile84, Ala28 ’, Gly49’, Ile50 ’and Arg87’ produced more than 1.0 kcal / mol And it is proved that CH-π, CH-O interaction and polarity are the main forms of their binding.It is expected that this result can provide theoretical guidance for the design of HIV-1 protease-targeted anti-AIDS drugs.