α‐Peptide–Oligourea Chimeras: Stabilization of Short α‐Helices by Non‐Peptide Helical Foldamers |
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| Authors: | Dr Juliette Fremaux Laura Mauran Dr Karolina Pulka‐Ziach Dr Brice Kauffmann Dr Benoit Odaert Dr Gilles Guichard |
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| Affiliation: | 1. Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33607 Pessac (France);2. CNRS, CBMN, UMR 5248, 33600 Pessac (France);3. UREkA, Sarl, 2 rue Robert Escarpit, 33607 Pessac (France);4. Present address: Faculty of Chemistry, University of Warsaw, Pasteura 1, 02‐093 Warsaw (Poland);5. Univ. Bordeaux, IECB, UMS 3033/US 001, 2 rue Escarpit, 33607 Pessac (France);6. CNRS, IECB, UMS 3033, 33600 Pessac (France);7. INSERM, IECB, US 001, 33600 Pessac (France);8. Univ. Bordeaux, CBMN, UMR 5248, All. Geoffroy Saint‐Hilaire, 33600 Pessac (France) |
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| Abstract: | Short α‐peptides with less than 10 residues generally display a low propensity to nucleate stable helical conformations. While various strategies to stabilize peptide helices have been previously reported, the ability of non‐peptide helical foldamers to stabilize α‐helices when fused to short α‐peptide segments has not been investigated. Towards this end, structural investigations into a series of chimeric oligomers obtained by joining aliphatic oligoureas to the C‐ or N‐termini of α‐peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an α‐helical conformation in the fused peptide segment. The remarkable compatibility of α‐peptides with oligoureas described here, along with the simplicity of the approach, highlights the potential of interfacing natural and non‐peptide backbones as a means to further control the behavior of α‐peptides. |
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| Keywords: | foldamers helices oligourea peptides X‐ray crystallography |
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