ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

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.

[img]
Preview
PDF
constrained.pdf

Download (2943Kb)

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
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.ernet.in/id/eprint/2878

Actions (login required)

View Item View Item