C. Roumestand et al., OLIGOMERIZATION OF PROTEGRIN-1 IN THE PRESENCE OF DPC MICELLES - A PROTON HIGH-RESOLUTION NMR-STUDY, FEBS letters, 421(3), 1998, pp. 263-267
Protegrins are members of a family of five Cys-rich naturally occurrin
g cationic antimicrobial peptides. The NMR solution structure of prote
grin-1 (PG-1) has been previously determined as a monomeric beta-hairp
in both in water and in dimethylsulfoxide solution, Protegrins are bac
tericidal peptides but their mechanism of action is still unknown. In
order to investigate the structural basis of their cytotoxicity, me st
udied the effect of Lipid micelles on the structure of PG-1. The NMR s
tudy 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 associa
tion between several dimers. (C) 1998 Federation of European Biochemic
al Societies.