抗菌肽LL-37与细菌膜POPG相互作用的分子动力学模拟研究  

Interaction between Antimicrobial Peptide LL-37 and Bacterial Membrane POPG by Molecular Dynamics Simulation

作　　者：毛文超[1,2] 赵立岭[1,3] 王吉华[1,3] 

机构地区：[1]德州学院山东省功能大分子生物物理重点实验室,济南250014 [2]山东师范大学生命科学学院,济南250014 [3]德州学院物理与电子信息学院,山东德州253023

出　　处：《德州学院学报》2016年第2期27-33,共7页Journal of Dezhou University

摘　　要：作为先天免疫系统的主要成分,人源抗菌肽LL-37在保护人类对抗疾病方面起了重要的角色.残基肽段17-29（FK-13）被认为是LL-37行使抗菌功能的核心区域,LL-37能对带负电的细菌膜产生破坏作用,其抗菌活性与二级结构的变化情况有关.用分子动力学模拟的方法研究了抗菌肽段FK-13与带负电的细菌膜POPG的相互作用.研究发现,库仑作用会使FK-13快速靠近膜的表面,然后像地毯一样覆盖在膜的表面;FK-13仍旧保持部分螺旋结构,并通过引起膜的扰动对膜产生破坏,以实现抗菌功能,而残基18-22是与膜作用的关键残基.研究FK-13与膜的相互作用,不仅可以从原子层面上了解LL-37对细菌膜作用的机理,也为基于LL-37设计高效抗菌药物提供帮助.As a major component of the innate immune system,human antimicrobial peptide LL-37 plays an important role in the protection of human resistance to disease.Residues 17-29（FK-13）are considered as the core area of LL-37 antimicrobial activity.LL-37 can damage bacterial membrane with negative.LL-37 antimicrobial activity is closely related to secondary structure changes.In this work,we studied the interaction between antimicrobial fragment FK-13 and of the bacterial membrane POPG by molecular dynamics simulation.The results show that the Coulomb interaction causes FK-13 close to the surface of the membrane rapidly and FK-13 can carpet the surface of the membrane.FK-13 has partial helix structure when it interacts with membrane.In addition,FK-13 can cause disturbance and destruction of the membrane and it is beneficial to exert antimicrobial activity.The residues 18-22are key residues in the membrane function.So the work is useful for us not only understand the changes of FK-13 conformation and its damage to the membrane but also provide a theoretical basis for FK-13 as a therapeutic application.

关 键 词：分子动力学模拟 抗菌肽段LL-37 细菌膜 

分 类 号：R378[医药卫生—病原生物学]