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Conformationally restricted formyl methionyl tripeptide chemoattractants: a three-dimensional structure-activity study of analogs incorporating a C alpha,alpha-dialkylated glycine at position 2

Toniolo, C and Crisma, M and Valle, G and Bonora, GM and Polinelli, S and Becker, EL and Freer, RJ (1989) Conformationally restricted formyl methionyl tripeptide chemoattractants: a three-dimensional structure-activity study of analogs incorporating a C alpha,alpha-dialkylated glycine at position 2. In: Pept Res, 2 (4). pp. 275-281.

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Official URL: http://www.ncbi.nlm.nih.gov/pubmed/2520765

Abstract

The conformationally restricted CHO-L-Met-Xxx-L-Phe-OY (where Xxx = Aib, Ac3c, Ac5c, Ac6c, and Ac7c; Y = H, Me) tripeptides, analogs of the chemoattractant CHO-L-Met-L-Leu-L-Phe-OH, have been synthesized in solution by classical methods and fully characterized. Compounds were compared to determine the combined effect of backbone conformational preferences and side-chain bulkiness on the relation of three-dimensional structure to biological activity. Each peptide was tested for its ability to induce granule enzyme secretion from rabbit peritoneal polymorphonuclear leukocytes. In parallel, a conformational analysis on the CHO-blocked peptide and their tertbutyloxycarbonylated synthetic precursors was performed in the crystal state and in solution using X-ray diffraction, infrared absorption, and 1H nuclear magnetic resonance. The biological and conformational data are discussed in relation to the proposed model of the chemotactic peptide receptor of rabbit neutrophils.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to National Center for Biotechnology Information.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 20 May 2010 06:36
Last Modified: 19 Sep 2010 06:00
URI: http://eprints.iisc.ernet.in/id/eprint/27236

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