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HIV-2蛋白酶已成为治疗艾滋病的一个重要药物靶标。作者采用分子动力学模拟并结合自由能计算,研究了抑制剂Amprenavir(AMP)与HIV-2蛋白酶的作用机制。研究结果表明范德华作用是AMP与HIV-2蛋白酶结合的主要力量。采用基于残基的自由能分解方法计算抑制剂-残基相互作用,结果表明疏水性的CH-π和CH-O相互作用驱动了抑制剂AMP与HIV-2蛋白酶的结合。作者期望这一研究结果能为抗艾滋病双重抑制剂的研发提供一定的理论指导。
HIV-2 protease has become an important drug target for the treatment of AIDS. The authors used molecular dynamics simulations combined with free energy calculations to study the mechanism of action of the inhibitor Amprenavir (AMP) and HIV-2 protease. The results show that van der Waals role is AMP and HIV-2 protease binding the main force. Inhibitor-residue interactions were calculated using a residue-based free energy decomposition approach and the results show that the hydrophobic CH-π and CH-O interactions drive the binding of inhibitor AMP to HIV-2 protease. The authors hope that the results of this study can provide some theoretical guidance for the development of double inhibitors against AIDS.