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α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers
Ist Teil von
Angewandte Chemie (International ed.), 2015-08, Vol.54 (34), p.9816-9820
Auflage
International ed. in English
Ort / Verlag
Weinheim: WILEY-VCH Verlag
Erscheinungsjahr
2015
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
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.
Conformational symbiosis: Non‐natural heterogeneous backbones obtained by fusing peptidomimetic urea‐based helical foldamers to either end of an α‐peptide segment fold into a helical structure, spanning the entire sequence in an uninterrupted manner. Only a few urea units are sufficient to propagate a helical conformation along short peptide segments.