Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study

被引：92

作者：

Roumestand, C

Louis, V

Aumelas, A

Grassy, G

Calas, B

Chavanieu, A

机构：

[1] Univ Montpellier 1, Fac Pharm, Ctr Biochim Struct, CNRS,UMR 9955,INSERM,U414, F-34060 Montpellier 1, France

[2] Ctr Rech Biochim Macromol, CNRS, ERS 155, F-34033 Montpellier, France

来源：

FEBS LETTERS | 1998年 / 421卷 / 03期

关键词：

protegrin; antimicrobial peptide; nuclear magnetic resonance structure; micelle;

D O I：

10.1016/S0014-5793(97)01579-2

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：

Protegrins are members of a family of five Cys-rich naturally occurring cationic antimicrobial peptides. The NMR solution structure of protegrin-1 (PG-1) has been previously determined as a monomeric beta-hairpin both in water and in dimethylsulfoxide solution, Protegrins are bactericidal peptides but their mechanism of action is still unknown. In order to investigate the structural basis of their cytotoxicity, me studied the effect of Lipid micelles on the structure of PG-1. The NMR study reported in the present work indicates that PG-1 adopts a dimeric structure when it binds to dodecylphosphocholine micelles, Moreover, the amide proton exchange study suggests the possibility of an association between several dimers. (C) 1998 Federation of European Biochemical Societies.

引用

页码：263 / 267

页数：5

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