Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides
Document Type
Article
Publication Date
2017
Digital Object Identifier (DOI)
https://doi.org/10.1021/jacs.7b03007
Abstract
New types of foldamer scaffolds are formidably challenging to design and synthesize, yet highly desirable as structural mimics of peptides/proteins with a wide repertoire of functions. In particular, the development of peptidomimetic helical foldamers holds promise for new biomaterials, catalysts, and drug molecules. Unnatural l-sulfono-γ-AApeptides were recently developed and shown to have potential applications in both biomedical and material sciences. However, d-sulfono-γ-AApeptides, the enantiomers of l-sulfono-γ-AApeptides, have never been studied due to the lack of high-resolution three-dimensional structures to guide structure-based design. Herein, we report the first synthesis and X-ray crystal structures of a series of 2:1 l-amino acid/d-sulfono-γ-AApeptide hybrid foldamers, and elucidate their folded conformation at the atomic level. Single-crystal X-ray crystallography indicates that this class of oligomers folds into well-defined right-handed helices with unique helical parameters. The helical structures were consistent with data obtained from solution 2D NMR, CD studies, and molecular dynamics simulations. Our findings are expected to inspire the structure-based design of this type of unique folding biopolymers for biomaterials and biomedical applications.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of the American Chemical Society, v. 139, issue 21, p. 7363-7369
Scholar Commons Citation
Teng, Peng; Ma, Ning; Cerrato, Darrell Cole; She, Fengyu; Odom, Timothy; Wang, Xiang; Ming, Li-June; Vaart, Arjan van der; Wojtas, Lukasz; Xu, Hai; and Cai, Jianfeng, "Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides" (2017). Chemistry Faculty Publications. 211.
https://digitalcommons.usf.edu/chm_facpub/211
