Accueil > Publications > Recherche par années > Années 1990 > 1997

Maget-Dana, R ; Brack, A ; Lelièvre, D

Amphiphilic peptides as models for protein-membrane interactions : interfacial behaviour of sequential Lys- and Leu-based peptides and their penetration into lipid monolayers

Supramolecular Science 4 (3-4) 365-368

par Administrateur - publié le

Abstract :

Synthetic peptides constructed with doublets of hydrophobic residues tandemly repeated with doublets of positively charged residues, (Leu-Lys-Lys-Leu)(n), were used as models for the study of protein-membrane interactions. Their behaviour has been compared with that of their strictly alternating iso peptides, (Leu-Lys)(n). Both peptides present a random coil structure in pure water. In saline solutions, (Leu-Lys-Lys-Leu)(n) peptides adopt an a-helical structure whereas (Leu-Lys)(n) transit into a ß-sheet structure.