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首页> 外文期刊>Biochemistry >Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2.
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Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2.

机译:抗菌肽magainin 2的膜选择性的分子基础。

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摘要

Magainin peptides, isolated from Xenopus skin, kill bacteria by permeabilizing their cell membranes whereas they do not lyse erythrocytes. To elucidate the rationale for this membrane selectivity, we compared the effects of the membrane lipid composition and the transmembrane potential on the membrane-lytic power of magainin 2 with that of hemolytic melittin. The activity of magainin to zwitterionic phospholipids constituting the erythrocyte surface was extremely weak compared with that of melittin, and acidic phospholipids are necessary for effective action. The presence of sterols reduced the susceptibility of the membrane to magainin. The generation of an inside-negative transmembrane potential enhanced magainin-induced hemolysis. We can conclude that the absence of any acidic phospholipids on the outer monolayer and the abundant presence of cholesterol, combined with the lack of the transmembrane potential, contribute to the protection of erythrocytes from magainin's attack.
机译:从非洲爪蟾皮中分离出来的洋甘菊肽通过使细胞膜通透来杀死细菌,而它们不裂解红细胞。为了阐明这种膜选择性的基本原理,我们比较了膜脂质成分和跨膜电位对magainin 2和溶血蜂毒素的膜溶解能力的影响。与蜂毒肽相比,麦胶苷对构成红细胞表面的两性离子磷脂的活性极弱,而酸性磷脂是有效作用所必需的。固醇的存在降低了膜对magainin的敏感性。内负跨膜电位的产生增强了由magainin引起的溶血作用。我们可以得出结论,在外单层上不存在任何酸性磷脂以及胆固醇的大量存在,再加上跨膜电位的缺乏,有助于保护红细胞免受麦加菌素的侵袭。

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