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Antimicrobial Peptides Increase Line Tension in Raft-Forming Lipid Membranes
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2024-07-17 , DOI: 10.1021/jacs.4c05377 Vladimir Rosenov Koynarev 1 , Kari Kristine Almåsvold Borgos 1 , Joachim Kohlbrecher 2 , Lionel Porcar 3 , Josefine Eilsø Nielsen 1 , Reidar Lund 1, 4
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2024-07-17 , DOI: 10.1021/jacs.4c05377 Vladimir Rosenov Koynarev 1 , Kari Kristine Almåsvold Borgos 1 , Joachim Kohlbrecher 2 , Lionel Porcar 3 , Josefine Eilsø Nielsen 1 , Reidar Lund 1, 4
Affiliation
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The formation of phase separated membrane domains is believed to be essential for the function of the cell. The precise composition and physical properties of lipid bilayer domains play crucial roles in regulating protein activity and governing cellular processes. Perturbation of the domain structure in human cells can be related to neurodegenerative diseases and cancer. Lipid rafts are also believed to be essential in bacteria, potentially serving as targets for antibiotics. An important question is how the membrane domain structure is affected by bioactive and therapeutic molecules, such as surface-active peptides, which target cellular membranes. Here we focus on antimicrobial peptides (AMPs), crucial components of the innate immune system, to gain insights into their interaction with model lipid membranes containing domains. Using small-angle neutron/X-ray scattering (SANS/SAXS), we show that the addition of several natural AMPs (indolicidin, LL-37, magainin II, and aurein 2.2) causes substantial growth and restructuring of the domains, which corresponds to increased line tension. Contrast variation SANS and SAXS results demonstrate that the peptide inserts evenly in both phases, and the increased line tension can be related to preferential and concentration dependent thinning of the unsaturated membrane phase. We speculate that the lateral restructuring caused by the AMPs may have important consequences in affecting physiological functions of real cells. This work thus shines important light onto the complex interactions and lateral (re)organization in lipid membranes, which is relevant for a molecular understanding of diseases and the action of antibiotics.
中文翻译：
抗菌肽增加筏形成脂质膜的线张力
据信相分离膜域的形成对于细胞的功能至关重要。脂质双层结构域的精确组成和物理特性在调节蛋白质活性和控制细胞过程中发挥着至关重要的作用。人类细胞结构域结构的扰动可能与神经退行性疾病和癌症有关。脂筏也被认为对细菌至关重要，有可能成为抗生素的靶标。一个重要的问题是膜结构域结构如何受到生物活性和治疗分子的影响，例如针对细胞膜的表面活性肽。在这里，我们重点关注天然免疫系统的重要组成部分——抗菌肽 (AMP)，以深入了解它们与含有结构域的模型脂膜的相互作用。使用小角中子/X 射线散射 (SANS/SAXS)，我们发现添加几种天然 AMP（indolicidin、LL-37、magainin II 和 aurein 2.2）会导致域的大幅增长和重组，这对应于以增加线张力。对比变化 SANS 和 SAXS 结果表明，肽在两个相中均匀插入，并且增加的线张力可能与不饱和膜相的优先和浓度依赖性变薄有关。我们推测AMP引起的横向重组可能对影响真实细胞的生理功能产生重要影响。因此，这项工作为脂膜中复杂的相互作用和横向（重组）组织提供了重要的线索，这与疾病和抗生素作用的分子理解相关。
更新日期：2024-07-17
中文翻译：
抗菌肽增加筏形成脂质膜的线张力
据信相分离膜域的形成对于细胞的功能至关重要。脂质双层结构域的精确组成和物理特性在调节蛋白质活性和控制细胞过程中发挥着至关重要的作用。人类细胞结构域结构的扰动可能与神经退行性疾病和癌症有关。脂筏也被认为对细菌至关重要，有可能成为抗生素的靶标。一个重要的问题是膜结构域结构如何受到生物活性和治疗分子的影响，例如针对细胞膜的表面活性肽。在这里，我们重点关注天然免疫系统的重要组成部分——抗菌肽 (AMP)，以深入了解它们与含有结构域的模型脂膜的相互作用。使用小角中子/X 射线散射 (SANS/SAXS)，我们发现添加几种天然 AMP（indolicidin、LL-37、magainin II 和 aurein 2.2）会导致域的大幅增长和重组，这对应于以增加线张力。对比变化 SANS 和 SAXS 结果表明，肽在两个相中均匀插入，并且增加的线张力可能与不饱和膜相的优先和浓度依赖性变薄有关。我们推测AMP引起的横向重组可能对影响真实细胞的生理功能产生重要影响。因此，这项工作为脂膜中复杂的相互作用和横向（重组）组织提供了重要的线索，这与疾病和抗生素作用的分子理解相关。
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