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Preface
Int. J. Mol. Sci. 2001, 2(1), 1-9; doi:10.3390/i2010001
Article

Theoretical Conformational Analysis of Chemotactic Peptides Formyl-Met-Leu-Phe-OMe and Formyl-Met-Acc6-Phe-OMe

1,* , 2, 3 and 3
1 Laboratoire de Recherche, Ecole Supérieur de Technologie, BP 8012 Oasis, Route d'El Jadida, Km 7, Casablanca, Marocco 2 Département de Chimie, Faculté des Sciences et Techniques Fes Sais, Université Sidi Mohamed Ben Abdellah B.P. 2202, Fes, Marocco 3 Laboratoire de Chimie Physique, Département de Chimie, Faculté des Sciences BP 5366- Maârif / Casablanca, Marocco
* Author to whom correspondence should be addressed.
Received: 4 October 2000 / Accepted: 15 December 2000 / Published: 2 February 2001
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Abstract

In order to investigate the proper peptide backbone conformation that is biologically active, the chemotactic peptides formyl-Met-Leu-Phe-OMe and formyl-Met-Acc6-Phe-OMe (Acc6 is the a-a disubstituted amino acid l-aminocyclohexane-1-carboxylic acid) were studied by the theoretical method PEPSEA. 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 a formyl group in the interaction with the receptor.
Keywords: Chemotactic peptide; conformation; a-a disubstituted amino acid; intramolecular hydrogen bond Chemotactic peptide; conformation; a-a disubstituted amino acid; intramolecular hydrogen bond
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Wazady, Y.; Hassani, C.A.; Lakhdar, M.; Ezzamarty, A. Theoretical Conformational Analysis of Chemotactic Peptides Formyl-Met-Leu-Phe-OMe and Formyl-Met-Acc6-Phe-OMe. Int. J. Mol. Sci. 2001, 2, 1-9.

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