Max Planck Institute of Colloids and Interfaces, Science Park Potsdam-Golm, Am Mühlenberg 1, 14476 Potsdam, Germany.
Max Planck Institute of Colloids and Interfaces, Science Park Potsdam-Golm, Am Mühlenberg 1, 14476 Potsdam, Germany.
Adv Colloid Interface Sci. 2017 Sep;247:521-532. doi: 10.1016/j.cis.2017.06.001. Epub 2017 Jun 5.
The interaction of antimicrobial peptides (AMPs) with biological membranes is in the focus of research since several years, and the most important features and modes of action of AMPs are described in this review. Different model systems can be used to understand such interactions on a molecular level. As a special example, we use 2D and 3D model membranes to investigate the interaction of the natural cyclic (Ar-1) and the synthetic linear molecule arenicin with selected amphiphiles and phospholipids. A panoply of sophisticated methods has been used to analyze these interactions on a molecular level. As a general trend, one observes that cationic antimicrobial peptides do not interact with cationic amphiphiles due to electrostatic repulsion, whereas with non-ionic amphiphiles, the peptide interacts only with aggregated systems and not with monomers. The interaction is weak (hydrophobic interaction) and requires an aggregated state with a large surface (cylindrical micelles). Anionic amphiphiles (as monomers or micelles) exhibit strong electrostatic interactions with the AMPs leading to changes in the peptide conformation. Both types of peptides interact strongly with anionic phospholipid monolayers with a preference for fluid layers. The interaction with a zwitterionic layer is almost absent for the linear derivative but measurable for the cyclic arenicin Ar-1. This is in accordance with biological experiments showing that Ar-1 forms well defined stable pores in phospholipid and lipopolysaccharide (LPS) membranes (cytotoxicity). The synthetic linear arenicin, which is less cytotoxic, does not affect the mammalian lipids to such an extent. The interaction of arenicin with bacterial membrane lipids is dominated by hydrogen bonding together with electrostatic and hydrophobic interactions.
抗菌肽（AMPs）与生物膜的相互作用是近年来研究的重点，本综述描述了 AMPs 的最重要特征和作用模式。可以使用不同的模型系统来在分子水平上理解这种相互作用。作为一个特殊的例子，我们使用 2D 和 3D 模型膜来研究天然环状（Ar-1）和合成线性分子arenicin 与选定的两亲物和磷脂的相互作用。已经使用了一系列复杂的方法来在分子水平上分析这些相互作用。一般来说，人们观察到阳离子抗菌肽由于静电排斥而不会与阳离子两亲物相互作用，而与非离子两亲物相互作用时，肽仅与聚集的系统相互作用而不与单体相互作用。相互作用较弱（疏水相互作用），并且需要具有大表面的聚集状态（圆柱状胶束）。阴离子两亲物（作为单体或胶束）与 AMP 表现出强烈的静电相互作用，导致肽构象发生变化。两种类型的肽都与阴离子磷脂单层强烈相互作用，对流体层有偏好。线性衍生物与两性离子层的相互作用几乎不存在，但环状 arenicin Ar-1 可测到。这与生物学实验一致，表明 Ar-1 在磷脂和脂多糖（LPS）膜（细胞毒性）中形成了明确的稳定孔。毒性较小的合成线性 arenicin 不会对哺乳动物脂质产生如此大的影响。arenicin 与细菌膜脂质的相互作用主要由氢键与静电和疏水相互作用共同主导。
