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Sulfono‐γ‐AApeptides as a New Class of Nonnatural Helical Foldamer
Author(s) -
Wu Haifan,
Qiao Qiao,
Hu Yaogang,
Teng Peng,
Gao Wenyang,
Zuo Xiaobing,
Wojtas Lukasz,
Larsen Randy W.,
Ma Shengqian,
Cai Jianfeng
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201406112
Subject(s) - foldamer , folding (dsp implementation) , circular dichroism , moiety , chemistry , monomer , sequence (biology) , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , organic chemistry , polymer , biochemistry , electrical engineering , engineering
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‐γ‐AApeptide foldamers of varying lengths. The crystal structure of the sulfono‐γ‐AApeptide monomer S6 illustrates the intrinsic folding propensity of sulfono‐γ‐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 well‐ defined helical conformation of sulfono‐γ‐AApeptides in solution containing as few as five building blocks. Future development of sulfono‐γ‐AApeptides may lead to new foldamers with discrete functions, enabling expanded application in chemical biology and biomedical sciences.