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Issue 2, 2018
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Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin

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Abstract

This paper reports conformational changes observed in cyclic bioactive peptides such as gramicidin S and avellanin upon incorporation of a pseudo-β (C9) Ant–DPro turn motif in their structural frameworks. Solution-state studies suggested that a synthetic gramicidin S analog exhibits a β-sheet conformation with C9 and C17 intramolecular hydrogen bonding patterns, while its truncated analog disturbs the β-sheet conformation. Structural details were obtained using a combination of CD studies, X-ray crystal structure studies and nOe-based MD simulation studies.

Graphical abstract: Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin

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Publication details

The article was received on 27 Sep 2017, accepted on 09 Dec 2017 and first published on 13 Dec 2017


Article type: Paper
DOI: 10.1039/C7NJ03701E
Citation: New J. Chem., 2018,42, 1197-1201
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    Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin

    A. S. Kotmale, E. Sangtani, R. G. Gonnade, D. Sarkar, S. Burade, P. R. Rajamohanan and G. J. Sanjayan, New J. Chem., 2018, 42, 1197
    DOI: 10.1039/C7NJ03701E

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