The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness

Peng Teng; Mengmeng Zheng; Darrell Cole Cerrato; Yan Shi; Mi Zhou; Songyi Xue; Wei Jiang; Lukasz Wojtas; Li-June Ming; Yong Hu; Jianfeng Cai

doi:10.1038/s42004-021-00496-0

Communications Chemistry (May 2021)

The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness

Peng Teng,
Mengmeng Zheng,
Darrell Cole Cerrato,
Yan Shi,
Mi Zhou,
Songyi Xue,
Wei Jiang,
Lukasz Wojtas,
Li-June Ming,
Yong Hu,
Jianfeng Cai

Affiliations

Peng Teng: Department of Chemistry, University of South Florida
Mengmeng Zheng: Department of Chemistry, University of South Florida
Darrell Cole Cerrato: Department of Chemistry, University of South Florida
Yan Shi: Department of Chemistry, University of South Florida
Mi Zhou: Department of Chemistry, University of South Florida
Songyi Xue: Department of Chemistry, University of South Florida
Wei Jiang: Department of Chemistry, University of South Florida
Lukasz Wojtas: Department of Chemistry, University of South Florida
Li-June Ming: Department of Chemistry, University of South Florida
Yong Hu: College of Engineering and Applied Science, Nanjing University
Jianfeng Cai: Department of Chemistry, University of South Florida

DOI: https://doi.org/10.1038/s42004-021-00496-0
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 9

Abstract

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Controlling the helical structure of peptide foldamers requires detailed understanding of the relationship between primary and secondary structure. Here the effect of monomer stoichiometry and configuration on the helical structures of peptide nucleic acids bearing sulfono pendants is examined.

Published in Communications Chemistry

ISSN: 2399-3669 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Chemistry
Website: https://www.nature.com/commschem

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