Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin. (20th December 2017)

• Record Type: Journal Article
• Authors: Kotmale, Amol S.; Sangtani, Ekta; Gonnade, Rajesh G.; Sarkar, Dhiman; Burade, Sachin; Rajamohanan, Pattuparambil R.; Sanjayan, Gangadhar J.
• Is Part Of: New journal of chemistry. Volume 42:Number 2(2018)
• Page Start: 1197
• Page End: 1201
• Publication Date: 2017-12-20
• Subjects: Chemistry -- Periodicals; Chimie -- Périodiques; 540
• DOI: 10.1039/c7nj03701e
• Languages: English
• ISSNs: 1144-0546

Abstract

Abstract : Conformational studies suggest that an Ant D Pro motif-incorporated synthetic gramicidin S analog retains β-sheet conformation, while its truncated analog avellanin disturbs the β-sheet conformation. 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– D Pro 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.