Action mechanism and structural requirements of the antimicrobial peptides, gaegurins

被引:47
|
作者
Won, Hyung-Sik [1 ]
Kang, Su-Jin [2 ]
Lee, Bong-Jin [2 ]
机构
[1] Konkuk Univ, Dept Biotechnol, Coll Biomed & Hlth Sci, Chungju 308701, Chungbuk, South Korea
[2] Seoul Natl Univ, Res Inst Pharmaceut Sci, Coll Pharm, Seoul 151742, South Korea
来源
关键词
Geagurin; Antimicrobial peptide; Rana box; Membrane binding; Structure-activity relationship; Nomenclature; RANA-ESCULENTA; AMPHIBIAN SKIN; MEMBRANE INTERACTION; MOLECULAR-CLONING; KOREAN FROG; BREVININ; 1E; RUGOSA; PROLINE; AGENTS; CDNAS;
D O I
10.1016/j.bbamem.2008.10.021
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Gaegurins (GGNs) are a family of cationic, alpha-helical, antimicrobial peptides that were isolated from a Korean frog, Glandirana emeljanovi (formerly classified as Rana rugosa) and represent one of the structurally well-characterized groups. Among six gaegurins, gaegurin 4 (renamed herein esculentin-2EM), gaegurin 5 (brevinin-1EMa), and gaegurin 6 (brevinin-1EMb) have been investigated comprehensively in terms of structure-activity relationships. In this paper, we first suggest renaming of gaegurins according to a recently raised rule of systematic nomenclature. Then, the current understanding of gaegurins is reviewed by summarizing their structure-activity relationships. in particular competing arguments on gaegurins are synthetically inspected. Finally their action mechanism and structural requirements will be discussed. Crown Copyright (C) 2008 Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1620 / 1629
页数:10
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