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Template-based stabilization of α-peptide helices with short accessory non-peptide helical foldamers fused either at the N- or C-terminus or at both ends of the peptide segment has been investigated by NMR spectroscopy in polar solvents and by X-ray diffraction. In this work, we focused on aliphatic N,N′-linked oligoureas that form predictable and well-defined helical structures akin to α-helices. Our results indicate that urea oligomers have the ability to enforce a peptide segment to adopt a well-defined α-helical structure and may suggest a general approach to stabilize short helical peptide epitopes for the development of modulators of protein–protein interactions

Stabilization of an α-helix by short adjacent accessory foldamers