Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study.
FEBS Lett
; 421(3): 263-7, 1998 Jan 16.
Article
em En
| MEDLINE
| ID: mdl-9468319
ABSTRACT
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, 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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Fosforilcolina
/
Proteínas
/
Anti-Infecciosos
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
França