Structure-activity relationship of an antibacterial peptide, maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata
Structure-activity relationship of an antibacterial peptide, maculatin 1.1, from the skin glands of the tree frog, Litoria genimaculata
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DOI：
10.1002/psc.560
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发表时间：
2004-07-01
影响因子：
2.1
通讯作者：
Aoyagi, H
中科院分区：
文献类型：
--
作者：
Niidome, T;Kobayashi, K;Aoyagi, H
斑蛋白1.1（Maculatin 1.1，Mac）是从树蛙（Litoria genimaculata）的背腺中分离的阳离子抗菌肽，并且具有GLFGVLAKVAAHVVPAIAAEHF-NH 2的序列。据报道，缺少Mac的N-末端两个残基的短肽没有活性。为了详细研究构效关系，合成了几种Mac类似物和相关短肽。CD测定表明，在阴离子脂质囊泡的存在下，所有肽都或多或少地呈现α-螺旋结构。比Mac碱性更强的类似物具有较强的抗菌和溶血活性，而缺少一个或两个末端残基的短肽表现出较弱或无活性。肽的外膜和内膜透化活性也随着肽链的缩短而降低。这些结果表明，Mac的整个链长是完全活性所必需的，并且肽的碱性极大地影响活性。版权所有（C）2004欧洲肽协会和约翰威利父子公司。
Maculatin 1.1 (Mac) is a cationic antibacterial peptide isolated from the dorsal glands of the tree frog, Litoria genimaculata, and has a sequence of GLFGVLAKVAAHVVPAIAEHF-NH2. A short peptide lacking the N-terminal two residues of Mac was reported to have no activity. To investigate the structure-activity relationship in detail, several analogs and related short peptides of Mac were synthesized. CD measurement showed that all the peptides took more or less an a-helical structure in the presence of anionic lipid vesicles. Analogs which are more basic than Mac had strong antibacterial and hemolytic activities, while short peptides lacking one or two terminal residues exhibited weak or no activity. Outer and inner membrane permeabilization activities of the peptides were also reduced with shortening of the peptide chain. These results indicate that the entire chain length of Mac is necessary for full activity, and the basicity of the peptides greatly affects the activity. Copyright (C) 2004 European Peptide Society and John Wiley Sons, Ltd.