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
相关论文
共 50 条
  • [41] The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action
    Chen, Rong
    Mark, Alan E.
    EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2011, 40 (04): : 545 - 553
  • [42] Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues
    Song, YM
    Park, Y
    Lim, SS
    Yang, ST
    Woo, ER
    Park, IS
    Lee, JS
    Kim, JI
    Hahm, KS
    Kim, Y
    Shin, SY
    BIOCHEMISTRY, 2005, 44 (36) : 12094 - 12106
  • [43] Mechanism of action of beta-stranded antimicrobial (KL)n model peptides
    Strandberg, Erik
    Schweigardt, Fabian
    Wadhwani, Parvesh
    Ulrich, Anne S.
    BIOPHYSICAL JOURNAL, 2023, 122 (03) : 369A - 369A
  • [44] Pore formation by hagfish intestinal antimicrobial peptides: Biophysical studies on mechanism of action
    Basanez, G
    Shinnar, AE
    Zimmerberg, J
    FASEB JOURNAL, 2000, 14 (08): : A1460 - A1460
  • [45] Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo
    Kumar, Prashant
    Kizhakkedathu, Jayachandran N.
    Straus, Suzana K.
    BIOMOLECULES, 2018, 8 (01)
  • [46] Mechanism of action of antimicrobial peptides: Different effects of B-sheet and a-helical peptides.
    Wang, W
    Orlov, D
    Azimov, R
    Lehrer, RI
    BIOPHYSICAL JOURNAL, 2001, 80 (01) : 538A - 538A
  • [47] Molecular mechanism of antimicrobial peptides
    Huang, Huey W.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2006, 231
  • [48] Antimicrobial peptides derived from different animals: comparative studies of antimicrobial properties, cytotoxicity and mechanism of action
    Han, Fei-Fei
    Liu, Yi-Fan
    Xie, Yong-Gang
    Gao, Yan-Hua
    Luan, Chao
    Wang, Yi-Zhen
    WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, 2011, 27 (08): : 1847 - 1857
  • [49] Antimicrobial peptides derived from different animals: comparative studies of antimicrobial properties, cytotoxicity and mechanism of action
    Fei-Fei Han
    Yi-Fan Liu
    Yong-Gang Xie
    Yan-Hua Gao
    Chao Luan
    Yi-Zhen Wang
    World Journal of Microbiology and Biotechnology, 2011, 27 : 1847 - 1857
  • [50] STRUCTURAL MODELING OF ANTIMICROBIAL PEPTIDES IN THE DATABASE OF ANTIMICROBIAL ACTIVITY AND STRUCTURE OF PEPTIDES
    Armstrong, Anthony
    Cruz, Phil
    Gabrielian, Andrei
    Chubinidze, Mindia
    Pirtskhalava, Malak
    Hurt, Darrell
    Rosenthal, Alex
    Tartakovsky, Mike
    PROTEIN SCIENCE, 2019, 28 : 172 - 172