MOLECULAR-BASIS FOR MEMBRANE SELECTIVITY OF AN ANTIMICROBIAL PEPTIDE, MAGAININ-2
MOLECULAR-BASIS FOR MEMBRANE SELECTIVITY OF AN ANTIMICROBIAL PEPTIDE, MAGAININ-2
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DOI：
10.1021/bi00010a034
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发表时间：
1995-03-14
期刊：
影响因子：
2.9
通讯作者：
MIYAJIMA, K
中科院分区：
文献类型：
--
作者：
MATSUZAKI, K;SUGISHITA, K;MIYAJIMA, K
从非洲爪蟾皮肤中分离出的maagainin肽，通过渗透细菌的细胞膜来杀死细菌，但它们不溶解红细胞。为了阐明这种膜选择性的基本原理，我们比较了膜脂组成和跨膜电位对magainin 2和溶血蜂毒素的溶膜能力的影响。与蜂毒素相比，蜂毒素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。甾醇的存在降低了膜对心肌蛋白的敏感性。内负跨膜电位的产生增强了抗凝血素诱导的溶血。我们可以得出这样的结论：外层缺乏任何酸性磷脂和大量的胆固醇，再加上缺乏跨膜电位，有助于保护红细胞免受抗体的攻击。
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.