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Oligomerization of protegrin‐1 in the presence of DPC micelles. A proton high‐resolution NMR study
Author(s) -
Roumestand Christian,
Louis Valérie,
Aumelas André,
Grassy Gérard,
Calas Bernard,
Chavanieu Alain
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01579-2
Subject(s) - chemistry , micelle , cationic polymerization , proton nmr , monomer , amide , peptide , nuclear magnetic resonance spectroscopy , antimicrobial peptides , cytotoxicity , stereochemistry , fluorine 19 nmr , biochemistry , organic chemistry , aqueous solution , in vitro , polymer
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.