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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Interaction of antimicrobial peptide protegrin with biomembranes.
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Interaction of antimicrobial peptide protegrin with biomembranes.

机译：抗菌肽protegrin与生物膜的相互作用。

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摘要

The antimicrobial peptide protegrin-1 (PG-1) interacts with membranes in a manner that strongly depends on membrane lipid composition. In this research we use an approach representing the outer layers of bacterial and red blood cell membranes with lipid monolayers and using a combination of insertion assay, epifluorescence microscopy, and surface x-ray scattering to gain a better understanding of antimicrobial peptide's mechanism of action. We find that PG-1 inserts readily into anionic dipalmitoyl-phosphatidylglycerol, palmitoyl-oleoyl-phosphatidylglycerol, and lipid A films, but significantly less so into zwitterionic dipalmitoyl-phosphatidylcholine, palmitoyl-oleoyl-phosphatidylcholine, and dipalmitoyl-phosphatidylethanolamine monolayers under similar experimental conditions. Epifluorescence microscopy shows that the insertion of PG-1 into the lipid layer results in the disordering of lipid packing; this disordering effect is corroborated by grazing incidence x-ray diffraction data. X-ray reflectivity measurements further point to the location of the peptide in the lipid matrix. In a pathologically relevant example we show that PG-1 completely destabilizes monolayer composed of lipid A, the major component in the outer membrane of Gram-negative bacteria, which is likely to be the mechanism by which PG-1 disrupts the outer membrane, thus allowing it to reach the target inner membrane.
机译：抗菌肽protegrin-1（PG-1）与膜相互作用的方式很大程度上取决于膜脂质的组成。在这项研究中，我们使用代表脂质和单层膜的细菌和红细胞膜外层的方法，并结合使用插入分析，表面荧光显微镜和表面X射线散射来更好地了解抗菌肽的作用机理。我们发现PG-1容易插入阴离子二棕榈酰-磷脂酰甘油，棕榈酰-油酰-磷脂酰甘油和脂质A膜中，但插入两性离子二棕榈酰-磷脂酰胆碱，棕榈酰-油酰-磷脂酰胆碱和二棕榈酰-磷脂酰单胺类似物条件下的插入量要少得多。 。荧光显微镜显示，PG-1插入脂质层会导致脂质堆积紊乱。掠入射X射线衍射数据证实了这种无序效应。 X射线反射率测量进一步指向肽在脂质基质中的位置。在病理相关的例子中，我们表明PG-1完全破坏了由脂质A（革兰氏阴性细菌外膜的主要成分）组成的单层的稳定性，这很可能是PG-1破坏外膜的机制，因此使其到达目标内膜。

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