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A Highly Active Chemotactic Peptide Analog Incorporating the Unusual Residue 1-Aminocyclohexanecarboxylic Acid at Position 2

Sukumara, M and Raja, Antony P and Balaram, P and Becker, EL (1985) A Highly Active Chemotactic Peptide Analog Incorporating the Unusual Residue 1-Aminocyclohexanecarboxylic Acid at Position 2. In: Biochemical and Biophysical Research Communications, 128 (1). pp. 339-344.

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Abstract

Analogs of chemotactic peptides (Formyl-Met-X-Phe-OMe) containing the stereochemically constrained residues \alpha-aminoisobutyric acid (Aib), 1-aminocyclopentanecarboxylic acid $\[(Acc^5\]$) and 1-aminocyclohexanecarboxylic acid $\[ (Acc^6\]$) at position 2 are compared with the parent sequence (X=Leu) for their ability to induce lysozyme release in rabbit neutrophils. The $\[Acc^6\]$ analog is about 78 times more active than the parent peptide, For-Met-Leu-Phe-OH, whereas Aib and $\[Acc^5\]$ analogs are approximately 3 and 2 times, respectively, less active than the parent peptide. NMR and model building studies clearly favour a $\[Met-Acc^6\]$ \beta-turn solution conformation in the $\[Acc^6\]$ analog, suggesting that the neutrophil receptor is capable of recognizing a folded peptide structure. The significant differences in the activities of the $\[Acc^5\]$ and $\[Acc^6\]$ analogs suggest an important role for the residue 2 sidechain in receptor interactions.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: H.S. Divakara
Date Deposited: 07 Jul 2008
Last Modified: 19 Sep 2010 04:46
URI: http://eprints.iisc.ac.in/id/eprint/14814

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