Sulfono‐γ‐AApeptides as a New Class of Nonnatural Helical Foldamer |
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| Authors: | Yaogang Hu Peng Teng Wenyang Gao Xiaobing Zuo Lukasz Wojtas Randy W. Larsen Shengqian Ma Jianfeng Cai |
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| Affiliation: | 1. Department of Chemistry, University of South Florida, 4202 E. Fowler Ave, Tampa, FL 33620 (USA);2. Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439 (USA) |
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| 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. |
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| Keywords: | 2D NMR spectroscopy helical foldamer peptidomimetics sulfono‐γ ‐AApeptides X‐ray crystal structure |
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