FREMAUX, Juliette; MAURAN, Laura; PULKA-ZIACH, Karolina; KAUFFMANN, Brice; ODAERT, Benoit; GUICHARD, Gilles

doi:10.1002/anie.201500901

Métadonnées

Afficher la notice complète

Licence d’utilisation du document

FREMAUX, Juliette

MAURAN, Laura

PULKA-ZIACH, Karolina

Langue

Article de revue

Ce document a été publié dans

Angewandte Chemie (International ed. in English). 2015, vol. 54, n° 34, p. 9816-20

Résumé en anglais

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 alpha-peptides.< Réduire

Métadonnées

Partager cette publication !

Licence d’utilisation du document

alpha-Peptide-Oligourea Chimeras: Stabilization of Short alpha-Helices by Non-Peptide Helical Foldamers

Langue

Ce document a été publié dans

Résumé en anglais

URI

DOI

Unités de recherche