Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin?
New Journal of Chemistry Pub Date: 2017-12-13 DOI: 10.1039/C7NJ03701E
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.
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Journal Name：New Journal of Chemistry
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CAS no.: 89640-58-4
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