Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation

Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
复制标题

DOI:
10.1016/s0006-3495(03)75103-0
复制
发表时间:
2003-06-01
影响因子:
3.4
通讯作者:
Huang, HW
Huang, HW
中科院分区:
生物学3区
文献类型:
--
作者:
Chen, FY;Lee, MT;Huang, HW

文献摘要

被引文献

相似文献

抗菌肽在脂质双层中有两种结合状态,即表面态S和成孔态I。从S态到成孔态的转变具有S型多肽浓度依赖关系,表明在多肽-膜相互作用中存在协同作用。在以前的一篇论文中,我们报道了在三种双层条件下测得的甲氧西林的转变。这些数据由一个自由能解释,该自由能考虑了多肽诱导的膜变薄效应。在这篇论文中,通过加入另一种类型的多肽蜂毒素来测试自由能的全部含义,这种多肽形成环状孔道,而不是像阿拉米西丁那样形成桶状孔道。用定向圆二色谱测量了S到我的跃迁。用X-射线衍射仪测定了膜的减薄效果。所有数据都与理论相符,表明膜变薄效应是多肽诱导成孔的一种可能机制。
Antimicrobial peptides have two binding states in a lipid bilayer, a surface state S and a pore-forming state I. The transition from the S state to the I state has a sigmoidal peptide-concentration dependence indicating cooperativity in the peptide-membrane interactions. In a previous paper, we reported the transition of alamethicin measured in three bilayer conditions. The data were explained by a free energy that took into account the membrane thinning effect induced by the peptides. In this paper, the full implications of the free energy were tested by including another type of peptide, melittin, that forms toroidal pores, instead of barrel-stave pores as in the case of alamethicin. The S-to-I transitions were measured by oriented circular dichroism. The membrane thinning effect was measured by x-ray diffraction. All data were in good agreement with the theory, indicating that the membrane thinning effect is a plausible mechanism for the peptide-induced pore formations.