分子对接研究壬基酚与N-乙酰氨基葡萄糖苷酶的相互作用  

Studies on Interaction of Nonyl-phenol with N-Acetylglucosaminidase by Molecular Docking Technology

作　　者：谢晓兰[1] 郑守真 高平章[1] 

机构地区：[1]福建省泉州师范学院化学与生命科学学院,福建泉州362000

出　　处：《宜春学院学报》2016年第3期1-5,共5页Journal of Yichun University

基　　金：国家自然科学青年基金项目(31302190);福建省自然科学基金项目(2012J01047)

摘　　要：目的:为了探究对壬基酚(p-NP)、邻壬基酚(o-NP)和间壬基酚(m-NP)三种异构体与N-乙酰氨基葡萄糖苷酶相互作用机制。方法:利用Autodock-tools 1.5.6和Open Babel软件对NAGase和壬基酚的构象进行处理,再用Autodock vina软件进行分子对接,用Py Mol和Discovery Studio 4.1分析两者对接的结合能量、结合方式和相互作用力。结果:模拟对接显示NAGase和壬基酚的三种异构体结合的能量分别为-5.7、-5.9、-5.9 kcal/mol;p-NP和NAGase通过疏水作用力结合,对接位点在NAGase B链的Trp306、Trp373和His169;o-NP和NAGase通过氢键和疏水作用力结合,对接位点在NAGase A链的Val592和Leu595,还有B链的Ala140、Pro132和Tyr136;m-NP和NAGase也通过氢键和疏水作用力结合,对接位点在NAGase B链的Tyr121、Trp306和Trp373。结论:壬基酚三种异构体和NAGase的相互作用机制有所差异。Objective： To study the interactive mechanism between nonyl -phenol（NP） Isomers（ p -NP, o -NPand m- NP） and N- acetylglucosaminidase（NAGase）. Methods： The conformations of NP and NAGase are pro-cessed by Autodock - tools 1.5.6 and OpenBabel, then the molecular docking of NP and NAGase is simulated byAutodock vina, finally the binding energy, binding sites and the interaction forces of NP and NAGase are analyzedby PyMol and Discovery Studio 4. 1. Results： Molecular docking shows that the energies of para -NP （p -NP）,ortho - NP （ o - NP）, meta- NP （ m - NP） binding with NAGase are - 5.7kcal/mol,5.9kcal/mol and 5.9kcal/tool, respectively, p- NP interacts with NAGase through hydrophobic force, and the binding sites are Trp306,Trp373 and His169 in B chain of NAGase. o - NP interacts with NAGase through hydrogen bond and hydrophobicforce, and the binding sites are Val592, Leu595 in A chain and Alal40, Pro132 and Tyr136 in B chain, m -NPinteracts with NAGase through hydrogen bond and hydrophobic forces as well, and the binding sites are Trp306,Trp373 and Tyrl21 in B chain of NAGase. Conclusions： The interaction mechanisms of three NP isomers and NA-Gase are different.

关 键 词：分子对接 作用机制 壬基酚 N-乙酰氨基葡萄糖苷酶 

分 类 号：X503.2[环境科学与工程—环境工程]