Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 34, Pages 9816-9820Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201500901
Keywords
foldamers; helices; oligourea; peptides; X-ray crystallography
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Funding
- CNRS
- Conseil Regional d'Aquitaine [20091102003]
- ANR [ANR-12BS07-0019]
- UREkA
- Univ. Bordeaux
- ANRT
- Marie Curie postdoctoral fellowship [PEOPLE-2010-IEF-273224-FOLDAPOP]
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Short alpha-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 alpha-helices when fused to short alpha-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 alpha-peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an alpha-helical conformation in the fused peptide segment. The remarkable compatibility of alpha-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 apeptides.
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