Specific interactions of the antimicrobial peptide cyclic β-sheet tachyplesin I with lipopolysaccharides

被引：74

作者：

Hirakura, Y

Kobayashi, S

Matsuzaki, K ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Biostudies, Kyoto 6068501, Japan

[2] Waseda Univ, Adv Res Ctr Human Sci, Tokyo 2020021, Japan

[3] Kyoto Univ, Grad Sch Pharmaceut Sci, Kyoto 6068501, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2002年 / 1562卷 / 1-2期

关键词：

antimicrobial peptide; tachyplesin I; lipopolysaccharide; binding isotherm; outer membrane; permeabilization;

D O I：

10.1016/S0005-2736(02)00358-9

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：

The cyclic beta-shect antimicrobial peptide tachyplesin I (T-SS) was found to show 280-fold higher affinity for lipopolysaccharides (LPS) compared with acidic phospholipids, whereas the linear alpha-helical peptide F5W-magainin 2 (MG2) could not discriminate between LPS and acidic phospholipids. The recognition site was the lipid A moiety and the cyclic structure was crucial to this specific binding, The cyclic structure also endowed the peptide with very rapid outer membrane (OM) permeabilization. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：32 / 36

页数：5

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