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Title: Right-Handed Helical Foldamers Consisting of De Novo d -AApeptides

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.

Authors:
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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NSFNIH
OSTI Identifier:
1377923
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of the American Chemical Society; Journal Volume: 139; Journal Issue: 21
Country of Publication:
United States
Language:
ENGLISH
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Teng, Peng, Ma, Ning, Cerrato, Darrell Cole, She, Fengyu, Odom, Timothy, Wang, Xiang, Ming, Li-June, van der Vaart, Arjan, Wojtas, Lukasz, Xu, Hai, and Cai, Jianfeng. Right-Handed Helical Foldamers Consisting of De Novo d -AApeptides. United States: N. p., 2017. Web. doi:10.1021/jacs.7b03007.
Teng, Peng, Ma, Ning, Cerrato, Darrell Cole, She, Fengyu, Odom, Timothy, Wang, Xiang, Ming, Li-June, van der Vaart, Arjan, Wojtas, Lukasz, Xu, Hai, & Cai, Jianfeng. Right-Handed Helical Foldamers Consisting of De Novo d -AApeptides. United States. doi:10.1021/jacs.7b03007.
Teng, Peng, Ma, Ning, Cerrato, Darrell Cole, She, Fengyu, Odom, Timothy, Wang, Xiang, Ming, Li-June, van der Vaart, Arjan, Wojtas, Lukasz, Xu, Hai, and Cai, Jianfeng. Tue . "Right-Handed Helical Foldamers Consisting of De Novo d -AApeptides". United States. doi:10.1021/jacs.7b03007.
@article{osti_1377923,
title = {Right-Handed Helical Foldamers Consisting of De Novo d -AApeptides},
author = {Teng, Peng and Ma, Ning and Cerrato, Darrell Cole and She, Fengyu and Odom, Timothy and Wang, Xiang and Ming, Li-June and van der Vaart, Arjan and Wojtas, Lukasz and Xu, Hai and Cai, Jianfeng},
abstractNote = {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.},
doi = {10.1021/jacs.7b03007},
journal = {Journal of the American Chemical Society},
number = 21,
volume = 139,
place = {United States},
year = {Tue May 16 00:00:00 EDT 2017},
month = {Tue May 16 00:00:00 EDT 2017}
}