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Controlling Helix Formation in the γ-Peptide Superfamily: Heterogeneous Foldamers with Urea/Amide and Urea/Carbamate Backbones

Authors


  • This work was supported by the CNRS, the University of Bordeaux (UB), the Conseil Régional d’Aquitaine, and ANR (Grant ANR-10-RPDOC-016). A fellowship from the University of Strasbourg (N.P.) is gratefully acknowledged. The crystallographic data have been collected at the IECB X-ray facility (UMS3033 CNRS and UB, US001 INSERM), at ESRF in Grenoble (France) and at the Swiss Light Source (SLS) in Villigen (Switzerland). Beamline scientists from ESRF ID29 and FIP BM30A are warmly acknowledged for beamtime and help during data collection. We thank Vincent Olieric for his support at the SLS synchrotron and Axelle Grélard for her assistance with NMR measurements.

Abstract

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One fold to rule them all: New heterogeneous aliphatic backbone foldamers belonging to the γ-peptide superfamily and containing various combinations of urea/amide (U/A) and urea/carbamate (U/C) units are reported. Structural studies at atomic resolution reveal hydrogen-bonded helical structures akin to that formed by cognate Un homooligomers.

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