CAJ | 학술논문

对艾滋病毒蛋白酶异位抑制剂体系和活性位抑制剂体系进行8ns的分子动力学模拟，用MM—PBSA方法分别计算了抑制剂与蛋白酶的结合自由能。异位抑制剂体系中抑制剂与蛋白酶的结合自由能为-90．30kcal／mol，活性位抑制剂体系中为-59．58kcal／mol。在异位抑制剂体系中分子片段4DX卡在蛋白酶的exo位，使蛋白酶活性位点附近残基的活动范围减小，有利于抑制剂被束缚在活性位点附近。异位抑制剂使体系刚性更强，更稳定，抑制剂与蛋白酶的结合更为牢固。
대애자병독단백매이위억제제체계화활성위억제제체계진행8ns적분자동역학모의，용MM—PBSA방법분별계산료억제제여단백매적결합자유능。이위억제제체계중억제제여단백매적결합자유능위-90．30kcal／mol，활성위억제제체계중위-59．58kcal／mol。재이위억제제체계중분자편단4DX잡재단백매적exo위，사단백매활성위점부근잔기적활동범위감소，유리우억제제피속박재활성위점부근。이위억제제사체계강성경강，경은정，억제제여단백매적결합경위뢰고。
We performed 8 ns of molecular dynamics simulation for the allosteric inhibitor and active site inhibitor system of HIV-1 protease. We also calculated their binding free energy with MM-PBSA. The free energy of inhibitor binding to protease is -90.30 kcal/mol in allosteric inhibitor system and the energy is -59.58 kcal/mol in active site inhibitor system. Molecular fragment 4DX stuck at protease exo site reduces the scope of residue activities near the active site in allosteric inhibitor system. It has favorable effect on the binding of inhibitor. Allosteric inhibitor makes a system more rigid and stable and the inhibitor binding to protease more firm.