Action of antimicrobial peptides: Two-state model

Action of antimicrobial peptides: Two-state model
复制标题

DOI:
10.1021/bi000946l
复制
发表时间:
2000-07-25
期刊:
影响因子:
2.9
通讯作者:
Huang, HW
Huang, HW
中科院分区:
生物学3区
文献类型:
--
作者:
Huang, HW

文献摘要

被引文献

相似文献

提出了一个两态模型的论点和实验证据,该模型解释了螺旋抗菌肽和P-折叠抗菌肽在与细胞质膜结合后的作用。每个肽都有两种不同的物理状态与脂类双层结合。在较低的肽/脂比(P/L)下,肽倾向于以非活性状态吸附在脂头基团区域。当P/L高于阈值P/L*时,该肽形成对细胞致命的多孔态。细胞对抗菌肽的敏感性取决于P/L的值,该值由细胞膜的脂组成决定。该模型合理地解释了实验结果,即不同细菌对一种多肽的敏感性与其结合亲和力没有直接关系,不同的多肽优先杀死不同的病原体,多肽对不同的真核细胞表现出不同程度的裂解活性。
The argument and experimental evidence are presented for a two-state model that explains the action of both helical and P-sheet antimicrobial peptides after they bind to the plasma membranes of cells. Each peptide has two distinct physical states of binding to lipid bilayers. At low peptide-to-lipid ratios (P/L), the peptide tends to adsorb in the lipid headgroup region in a functionally inactive state. At a P/L above a threshold value P/L*, the peptide forms a multiple-pore state that is lethal to a cell. The susceptibility of a cell to an antimicrobial peptide depends on the value of P/L* that is determined by the lipid composition of the cell membrane. This model provides plausible explanations for the experimental findings that the susceptibility of different bacteria to a peptide is not directly correlated to its binding affinity, different peptides preferentially kill different pathogens, and peptides exhibit varying levels of lytic activity against different eukaryotic cells.