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helical structures, hydrogen bonds, left-handed foldamers, peptidomimetics, X-ray diffraction

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The development of peptidomimetic helical foldamers with a wide repertoire of functions is of significant interest. Herein, we report the X‐ray crystal structures of a series of homogeneous l‐sulfono‐γ‐AA foldamers and elucidate their folding conformation at the atomic level. Single‐crystal X‐ray crystallography revealed that this class of oligomers fold into unprecedented dragon‐boat‐shaped and unexpected left‐handed helices, which are stabilized by the 14‐hydrogen‐bonding pattern present in all sequences. These l‐sulfono‐γ‐AApeptides have a helical pitch of 5.1 Å and exactly four side chains per turn, and the side chains lie perfectly on top of each other along the helical axis. 2D NMR spectroscopy, computational simulations, and CD studies support the folding conformation in solution. Our results provide a structural basis at the atomic level for the design of novel biomimetics with a precise arrangement of functional groups in three dimensions.

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Angewandte Chemie International Edition, v. 57, issue 31, p. 9916-9920

This is the pre-peer reviewed version of the following article: F. She, P. Teng, A. Peguero-Tejada, M. Wang, N. Ma, T. Odom, M. Zhou, E. Gjonaj, L. Wojtas, A. van der Vaart, J. Cai, Angew. Chem. Int. Ed. 2018, 57, 9916., which has been published in final form at 10.1002/anie.201805184. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.