# 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 Copyright of this article belongs to Elsevier. Division of Biological Sciences > Molecular Biophysics Unit H.S. Divakara 07 Jul 2008 19 Sep 2010 04:46 http://eprints.iisc.ac.in/id/eprint/14814