CAJ | 학술논문

为分析和解释2个小分子抑制剂ADS-J1和ADS-J2与艾滋病病毒蛋白gp41的抑制机理,通过采用理论计算的方式把抑制剂和gp41蛋白疏水性空穴对接,得到了可能的结合方式,并通过采用分子动力学和MM/PBSA相结合的方法,确定蛋白质和抑制剂的具体结合方式和结合自由能,并且获得了抑制剂和蛋白的精确结合构型和相互作用力,明确了抑制剂和蛋白质之间的抑制机理.理论研究证实了相关实验的推测,并且为以后设计新型的gp41小分子抑制剂提供了良好的基础.
위분석화해석2개소분자억제제ADS-J1화ADS-J2여애자병병독단백gp41적억제궤리,통과채용이론계산적방식파억제제화gp41단백소수성공혈대접,득도료가능적결합방식,병통과채용분자동역학화MM/PBSA상결합적방법,학정단백질화억제제적구체결합방식화결합자유능,병차획득료억제제화단백적정학결합구형화상호작용력,명학료억제제화단백질지간적억제궤리.이론연구증실료상관실험적추측,병차위이후설계신형적gp41소분자억제제제공료량호적기출.
In order to analyze and explain the mechanism of the two small inhibitors (ADS-J1 and ADS-J2) binding to HIV-1 gp41,a computational study is carried out to help identifying possible binding modes by docking these compounds onto the hydrophobic pocket on gp41 and characterize structures of binding complexes.The binding interactions of gp41-molecule and free energies of binding are obtained through molecular dynamics simulation and molecular mechanic/PoissonBoitzmann surface area ( MM/PBSA ) calculation.Specific molecular interactions in the gp41-inhibitor complexes are identified.The present computational study complements the corresponding experimental investigation and helps establish a good starting point for further refinement of small molecular gp41 inhibitors.