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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Effect of N-terminal acetylation on lytic activity and lipid-packing perturbation induced in model membranes by a mastoparan-like peptide
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Effect of N-terminal acetylation on lytic activity and lipid-packing perturbation induced in model membranes by a mastoparan-like peptide

机译：N-末端乙酰化对乳腺素样肽模型膜中裂解活性和脂质包装扰动的影响

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摘要

L1A (IDGLKAIWKKVADLLKNT-NH2) is a peptide that displays a selective antibacterial activity to Gram-negative bacteria without being hemolytic. Its lytic activity in anionic lipid vesicles was strongly enhanced when its N terminus was acetylated (ac-L1A). This modification seems to favor the perturbation of the lipid core of the bilayer by the peptide, resulting in higher membrane lysis. In the present study, we used lipid monolayers and bilayers as membrane model systems to explore the impact of acetylation on the L1A lytic activity and its correlation with lipid-packing perturbation. The lytic activity investigated in giant unilamellar vesicles (GUVs) revealed that the acetylated peptide permeated the membrane at higher rates compared with L1A, and modified the membrane's mechanical properties, promoting shape changes. The peptide secondary structure and the changes in the environment of the tryptophan upon adsorption to large unilamellar vesicles (LUVs) were monitored by circular dichroism (CD) and red-edge excitation shift experiments (REES), respectively. These experiments showed that the N-terminus acetylation has an important effect on both, peptide secondary structure and peptide insertion into the bilayer. This was also confirmed by experiments of insertion into lipid monolayers. Compression isotherms for peptide/lipid mixed films revealed that ac-L1A dragged lipid molecules to the more disordered phase, generating a more favorable environment and preventing the lipid molecules from forming stiff films. Enthalpy changes in the main phase transition of the lipid membrane upon peptide insertion suggested that the acetylated peptide induced higher impact than the non-acetylated one on the thermotropic behavior of anionic vesicles.
机译：L1A（IDGLKaiwkkvadllknt-NH2）是一种肽，其显示在没有溶血的革兰氏阴性细菌的选择性抗菌活性。当其N末端是乙酰化（AC-L1A）时，其在阴离子脂质囊泡中的裂解活性强烈地增强。这种改性似乎有利于通过肽的双层脂质芯的扰动，从而产生更高的膜裂解。在本研究中，我们使用脂质单层和双层作为膜模型系统，以探讨乙酰化对L1A裂解活性的影响及其与脂质包装扰动的相关性。在巨型Unilamellar囊泡（GUV）中研究的裂解活性显示，与L1A相比，乙酰化肽以较高的速率渗透膜，并改性膜的机械性能，促进形状变化。通过圆形二色（CD）和红边激发换档实验（REES），监测肽二分粒子（LUVS）对大型Unilamellar囊泡（LUV）时对色氨酸的肽的二级结构及其变化。这些实验表明，N-末端乙酰化对两者，肽二次结构和肽插入双层具有重要作用。这也通过插入脂质单层的实验来证实。用于肽/脂质混合膜的压缩等温线显示，AC-L1A拖动脂质分子以更紊乱的相，产生更有利的环境并防止脂质分子形成刚性膜。肽插入时脂质膜的主相转变的焓变化表明，乙酰化肽比阴离子囊泡的热统计行为诱导比非乙酰化的肽更高的冲击。

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