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

FEBS Letters

Louis, Valérie¹  Aumelas, André¹  Roumestand, Christian¹  Chavanieu, Alain²  Grassy, Gérard¹  Calas, Bernard² 

[1] Centre de Biochimie Structurale, CNRS-UMR 9955, INSERM-U414, Université de Montpellier I, Faculté de Pharmacie, 15 Avenue Charles Flahault, 34060 Montpellier Cedex 1, France;Centre de Recherche de Biochimie Macromoléculaire, CNRS-ERS 155, BP5051 route de Mende, 34033 Montpellier Cedex 2, France

关键词: Protegrin;    Antimicrobial peptide;    Nuclear magnetic resonance structure;    Micelle;    NOE;    nuclear Overhauser enhancement;    NOESY;    nuclear Overhauser enhancement spectroscopy;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/S0014-5793(97)01579-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 β-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, we 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.

【 授权许可】

Unknown