自旋标记的抗菌肽 magainin 2 和 PGLa 在脂质双层膜中的自组装

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Victoria N. Syryamina , Christopher Aisenbrey , Maria Kardash , Sergei A. Dzuba , Burkhard Bechinger
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引用次数: 0

摘要

阳离子抗菌肽 PGLa 和 magainin 2(Mag2)因其抗菌活性以及在抗菌和膜渗漏试验中的协同增效作用而闻名。要在联合疗法中进一步使用多肽,就必须了解单个多肽及其混合物的作用机制。在此,我们应用电子顺磁共振(EPR)、双电子-电子共振(DEER,也称为 PELDOR)和电子自旋回波包络调制(ESEEM)光谱来研究自旋标记的 PGLa 和 Mag2 在 POPE/POPG 膜中的自组装和定位,肽/脂比率(P/L)范围从 1/1500 到 1/50。EPR 和 DEER 数据显示,这两种肽都倾向于组织成簇,在最低的肽/脂摩尔比 1/1500 (0.067 摩尔%)时就已经出现了这种情况。对于单个肽而言,这些簇非常致密,分子间距约为∼2 nm。在有增效肽伴侣的情况下,这些同簇会转化为稀释脂质的异簇。这些簇的特点是局部表面密度比随机分布的预期高出数倍。ESEEM 数据表明,与同簇相比,异簇中肽的插入深度略有不同。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Self-assembly of spin-labeled antimicrobial peptides magainin 2 and PGLa in lipid bilayers

Self-assembly of spin-labeled antimicrobial peptides magainin 2 and PGLa in lipid bilayers

The cationic antimicrobial peptides PGLa and magainin 2 (Mag2) are known for their antimicrobial activity and synergistic enhancement in antimicrobial and membrane leakage assays. Further use of peptides in combinatory therapy requires knowledge of the mechanisms of action of both individual peptides and their mixtures. Here, electron paramagnetic resonance (EPR), double electron-electron resonance (DEER, also known as PELDOR) and electron spin echo envelope modulation (ESEEM) spectroscopies were applied to study self-assembly and localization of spin-labeled PGLa and Mag2 in POPE/POPG membranes with a wide range of peptide/lipid ratios (P/L) from ∼1/1500 to 1/50. EPR and DEER data showed that both peptides tend to organize in clusters, which occurs already at the lowest peptide/lipid molar ratio of 1/1500 (0.067 mol%). For individual peptides, these clusters are quite dense with intermolecular distances of the order of ∼2 nm. In the presence of a synergistic peptide partner, these homo-clusters are transformed into lipid-diluted hetero-clusters. These clusters are characterized by a local surface density that is several times higher than expected from a random distribution. ESEEM data indicate a slightly different insertion depth of peptides in hetero-clusters when compared to homo-clusters.

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来源期刊
Biophysical chemistry
Biophysical chemistry 生物-生化与分子生物学
CiteScore
6.10
自引率
10.50%
发文量
121
审稿时长
20 days
期刊介绍: Biophysical Chemistry publishes original work and reviews in the areas of chemistry and physics directly impacting biological phenomena. Quantitative analysis of the properties of biological macromolecules, biologically active molecules, macromolecular assemblies and cell components in terms of kinetics, thermodynamics, spatio-temporal organization, NMR and X-ray structural biology, as well as single-molecule detection represent a major focus of the journal. Theoretical and computational treatments of biomacromolecular systems, macromolecular interactions, regulatory control and systems biology are also of interest to the journal.
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