MAURAN, Laura; KAUFFMANN, Brice; ODAERT, Benoit; GUICHARD, Gilles

doi:10.1016/j.crci.2015.07.003

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COMPTES RENDUS CHIMIE. 2016, vol. 19, n° 1-2, p. 123-131

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Template-based stabilization of alpha-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 alpha-helices. Our results indicate that urea oligomers have the ability to enforce a peptide segment to adopt a well-defined alpha-helical structure and may suggest a general approach to stabilize short helical peptide epitopes for the development of modulators of protein protein interactions. (C) 2015 Academie des sciences. Published by Elsevier Masson SAS. This is an open access article under the CC BY-NC-ND license.< Réduire

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Stabilization of an alpha-helix by short adjacent accessory foldamers

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