08年的GROMACS肽膜作用文章（免费分享）
COARSE-GRAINED SIMULATIONS OF THE MEMBRANE-ACTIVE ANTIMICROBIAL PEPTIDE MACULATIN 1.1
Abstract：
Maculatin 1.1 (M1.1) is a membrane-active antimicrobial peptide (AMP) from an Australian tree frog, which forms a kinked amphipathic α-helix in the presence of a lipid bilayer or bilayermimetic environment. To help understand its mechanism of membrane-lytic activity, we have performed a total of ~8 μs of coarse-grained molecular dynamics simulations of M1.1 in the presence of zwitterionic phospholipid membranes. Several systems were simulated in which the peptide:lipid ratio was varied. At a low peptide:lipid ratio, M1.1 adopted a kinked, membraneinterfacial location, consistent with experiment. At higher peptide:lipid ratios, we observed spontaneous, cooperative membrane insertion of M1.1 peptide aggregates. The minimum size for formation of a TM aggregate was just four peptides. The absence of a simple and well-defined central channel, along with the exclusion of lipid headgroups from the aggregates, suggests that a pore-like model is an unlikely explanation for the mechanism of membrane lysis by M1.1. We also performed an extended 1.25 μs simulation of the permeabilization of a complete liposome by multiple peptides. Consistent with the simpler bilayer simulations, formation of monomeric interfacial peptides and transmembrane peptide clusters was observed. In contrast, major structural changes were observed in the vesicle membrane, implicating induced membrane curvature in the mechanism of AMP lysis. This contrasted with the behaviour of the non-poreforming model peptide WALP23, which inserted into the vesicle to form extended clusters of transmembrane α-helices with relatively little perturbation of bilayer properties.
08年的GROMACS肽膜作用文章，下载时已接收但还未正式出版。本文对抗菌肽Maculatin 1.1（21肽）作了8微秒的模拟（好巨大的运算量），已揭示其破坏细胞膜结构的机理。
[ 本帖最后由 geffery 于 2008-8-29 19:05 编辑 ]
附件: 您所在的用户组无法下载或查看附件
搜索更多相关主题的帖子:
多肽 细胞膜 GMX
