蜂毒肽
膜
肽
生物物理学
抗菌肽
化学
马加宁
脂质双层
抗菌剂
双层
磷脂
生物膜
动力学(音乐)
生物化学
生物
作者
Cheng Xu,Wendong Ma,Kang Wang,Kejie He,Zhonglan Chen,Jiaojiao Liu,Kai Yang,Bing Yuan
标识
DOI:10.1021/acs.jpclett.0c01169
摘要
Many fundamental biological processes occur on cell membranes, and a typical example is the membrane permeabilization by peptides for an antimicrobial purpose. Previous studies of the underlying mechanism mostly focus on structural changes of membranes and peptides during their interactions. Herein, from a new perspective of single-molecule dynamics, the real-time three-dimensional motions of individual phospholipid and peptide molecules were monitored, and specifically, their correlation with the membrane poration function of melittin, a most representative natural antimicrobial peptide, was studied. We found that the adsorption and accumulation of melittin on the membrane surface significantly sped up the lateral diffusion of lipids surrounding the peptides, which in turn facilitated the peptide insertion at such heterogeneous regions. A unique U-bending pathway of melittin during membrane insertion and the ultimate formation of toroidal pores with dynamical translocations of peptides and lipids with several metastable states between the two leaflets of bilayer were observed.
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