CAJ | 학술논문

本文使用分子对接方法和MM/PBSA方法计算抑制剂BEG与 HIV-1蛋白酶的结合自由能，结果表明范德华相互作用主宰了BEG与 HIV-1蛋白酶的结合，还证明分子对接采用的分子力场相比于Amber12力场更适合于BEG-HIV蛋白酶系统。本文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，结果表明残基Leu23、Gly49、Ile50、Val82、Ile84、Asp25′、Gly27′、Ala28′、Gly49′、Ile50′和Ile84′与BEG产生了较强的相互作用，同时也证明CH-π和CH-O相互作用驱动了抑制剂BEG与HIV-1蛋白酶的结合。我们期望这个研究能为艾滋病治疗药物的合理化设计提供理论上的指导和实验上的参考。
본문사용분자대접방법화MM/PBSA방법계산억제제BEG여 HIV-1단백매적결합자유능，결과표명범덕화상호작용주재료BEG여 HIV-1단백매적결합，환증명분자대접채용적분자력장상비우Amber12력장경괄합우BEG-HIV단백매계통。본문채용기우잔기적자유능분해방법계산료억제제-잔기상호작용，결과표명잔기Leu23、Gly49、Ile50、Val82、Ile84、Asp25′、Gly27′、Ala28′、Gly49′、Ile50′화Ile84′여BEG산생료교강적상호작용，동시야증명CH-π화CH-O상호작용구동료억제제BEG여HIV-1단백매적결합。아문기망저개연구능위애자병치료약물적합이화설계제공이론상적지도화실험상적삼고。
In this work ,the molecular docking method and molecular mechanics Poisson-Boltzmann sur-face area (MM/PBSA) method were performed to calculate the binding free energy of the inhibitor BEG to HIV-1 protease . T he results suggest that Van der Waals energy controles the binding of BEG to HIV-1 protease .Also ,the force fields adopted in the molecular docking program is more adaptive to the BEG-HIV protease system than Amber force field .In addition ,the residue-based free enenrgy decompo-sition method was applied to compute the inhibitor-residue interaction .The results suggest that the resi-dues Leu23、Gly49、Ile50、Val82、Ile84、Asp25′、Gly27′、Ala28′、Gly49′、Ile50′and Ile84′produce stronger interaction with BEG .This work also proves that the CH-π and CH-O interactions drive the binding of BEG to HIV-1 protease .We expect this work can provide some helpful contributions for the design of high affinity inhibitors .