Conformationally constrained chemotactic peptide analogs of high biological activity

Iqbal, M and Balaram, P and Showell, HJ and Freer, RJ and Becker, EL (1984) Conformationally constrained chemotactic peptide analogs of high biological activity. In: FEBS Letters, 165 (2). pp. 171-174.

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Abstract

The stereochemically constrained chemotactic peptide analogs, formylmethionyl-\alpha-aminoisobutyrylphenylalanine (formyl-Met-Aib-Phe-OH) and formylmethionylcycloleucinylphenylalanine (formyl-Met-Cyl-Phe-OH) are highly effective in inducing lysosomal enzyme release from rabbit neutrophils. NMR studies of the ${Aib}^2$ analog in ${({CD}_3)}_2SO$ favor a folded conformation in which the Phe NH group is inaccessible to solvent. Intramolecularly hydrogen-bonded conformations involving a Met-Aib-\beta-turn or a \gamma-turn centered at ${Aib}^2$ are considered. The results suggest that folded conformations may allow highly active interactions with the neutrophil formylpeptide receptor.

Item Type:	Journal Article
Publication:	FEBS Letters
Publisher:	Elsevier
Additional Information:	Copyright for this article belongs to Elsevier Science Ltd.
Keywords:	chemotactic peptide;neutrophil;chemotaxis;formylpeptide
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	10 Mar 2005
Last Modified:	19 Sep 2010 04:18
URI:	http://eprints.iisc.ac.in/id/eprint/2878

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