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Title: Sulfono-g-AApeptides as a New Class of Nonnatural Helical Foldamer

Abstract

Foldamers offer an attractive opportunity for the design of novel molecules that mimic the structures and functions of proteins and enzymes including biocatalysis and biomolecular recognition. Herein we report a new class of nonnatural helical sulfono-g-AApeptide foldamers of varying lengths. The crystal structure of the sulfono-g-AApeptide monomer S6 illustrates the intrinsic folding propensity of sulfono-g-AApeptides, which likely originates from the bulkiness of tertiary sulfonamide moiety. The two-dimensional solution NMR spectroscopy data for the longest sequence S1 demonstrates a 10/16 right-handed helical structure. Optical analysis using circular dichroism further supports welldefined helical conformation of sulfono-g-AApeptides in solution containing as few as five building blocks. Future development of sulfono-g-AApeptides may lead to new foldamers with discrete functions, enabling expanded application in chemical biology and biomedical sciences.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Science Foundation (NSF)
OSTI Identifier:
1240293
DOE Contract Number:
AC02-06CH11357
Resource Type:
Journal Article
Resource Relation:
Journal Name: Chemistry - A European Journal (Online); Journal Volume: 21; Journal Issue: 6
Country of Publication:
United States
Language:
English
Subject:
2D NMR spectroscopy; Helical foldamer; peptidomimetics; sulfono-y-AApeptides; x-ray crystal structure

Citation Formats

Wu, Haifan, Qiao, Qiao, Hu, Yaogang, Teng, Peng, Gao, Wenyang, Zuo, Xiaobing, Wojtas, Lukasz, Larsen, Randy W., Ma, Shengqian, and Cai, Jianfeng. Sulfono-g-AApeptides as a New Class of Nonnatural Helical Foldamer. United States: N. p., 2015. Web. doi:10.1002/chem.201406112.
Wu, Haifan, Qiao, Qiao, Hu, Yaogang, Teng, Peng, Gao, Wenyang, Zuo, Xiaobing, Wojtas, Lukasz, Larsen, Randy W., Ma, Shengqian, & Cai, Jianfeng. Sulfono-g-AApeptides as a New Class of Nonnatural Helical Foldamer. United States. doi:10.1002/chem.201406112.
Wu, Haifan, Qiao, Qiao, Hu, Yaogang, Teng, Peng, Gao, Wenyang, Zuo, Xiaobing, Wojtas, Lukasz, Larsen, Randy W., Ma, Shengqian, and Cai, Jianfeng. Mon . "Sulfono-g-AApeptides as a New Class of Nonnatural Helical Foldamer". United States. doi:10.1002/chem.201406112.
@article{osti_1240293,
title = {Sulfono-g-AApeptides as a New Class of Nonnatural Helical Foldamer},
author = {Wu, Haifan and Qiao, Qiao and Hu, Yaogang and Teng, Peng and Gao, Wenyang and Zuo, Xiaobing and Wojtas, Lukasz and Larsen, Randy W. and Ma, Shengqian and Cai, Jianfeng},
abstractNote = {Foldamers offer an attractive opportunity for the design of novel molecules that mimic the structures and functions of proteins and enzymes including biocatalysis and biomolecular recognition. Herein we report a new class of nonnatural helical sulfono-g-AApeptide foldamers of varying lengths. The crystal structure of the sulfono-g-AApeptide monomer S6 illustrates the intrinsic folding propensity of sulfono-g-AApeptides, which likely originates from the bulkiness of tertiary sulfonamide moiety. The two-dimensional solution NMR spectroscopy data for the longest sequence S1 demonstrates a 10/16 right-handed helical structure. Optical analysis using circular dichroism further supports welldefined helical conformation of sulfono-g-AApeptides in solution containing as few as five building blocks. Future development of sulfono-g-AApeptides may lead to new foldamers with discrete functions, enabling expanded application in chemical biology and biomedical sciences.},
doi = {10.1002/chem.201406112},
journal = {Chemistry - A European Journal (Online)},
number = 6,
volume = 21,
place = {United States},
year = {Mon Feb 02 00:00:00 EST 2015},
month = {Mon Feb 02 00:00:00 EST 2015}
}