Youssef Wazady
Laboratoire de recherche, Ecole Supérieur de Technologie, BP 8012 Oasis, Route d'El Jadida, Km 7, Casablanca-Maroc

Chakib Ameziane Hassani
Département de chimie, faculté des sciences et techniques Fes sais, Université Sidi Mohamed Ben Abdellah BP 2202, Fes-Maroc

Mahjoub Lakhdar, Aziz Ezzamarty
Département de chimie, Faculté des Sciences BP 5366 Maârif / Casablanca-Maroc
 

ABSTRACT

The chemotactic peptides formyl-Met-Leu-Phe-OMe and formyl-Met-Acc5-Phe-OMe (Acc5 is the a-a disubstituted amino acid l-aminocyclopentane-1-carboxylic acid) were studied by the theoretical method PEPSEA in order to investigate the proper peptide backbone conformation that is biologically active. This study shows that the parent peptide formyl-Met-Leu-Phe-OMe has a flexible structure, and that the other conformationally constrained peptide has a tendency to form the b turn structure. It also gives evidence against the hypothesis proposing the importance of formyl group in the interaction with the receptor.