Controlling Helix Formation in the γ-Peptide Superfamily: Heterogeneous Foldamers with Urea/Amide and Urea/Carbamate Backbones

One fold to rule them all: New heterogeneous aliphatic backbone foldamers belonging to the γ‐peptide superfamily and containing various combinations of urea/amide (U/A) and urea/carbamate (U/C) units are reported. Structural studies at atomic resolution reveal hydrogen‐bonded helical structures akin...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie 2013-04, Vol.52 (15), p.4147-4151
Hauptverfasser:	Pendem, Nagendar, Nelli, Yella Reddy, Douat, Céline, Fischer, Lucile, Laguerre, Michel, Ennifar, Eric, Kauffmann, Brice, Guichard, Gilles
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides - chemistry Carbamates - chemistry Chemical Sciences foldamers helical structures Models, Molecular Other Peptides - chemical synthesis Peptides - chemistry peptidomimetics Protein Folding Protein Structure, Secondary Urea - chemistry X-ray diffraction
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	One fold to rule them all: New heterogeneous aliphatic backbone foldamers belonging to the γ‐peptide superfamily and containing various combinations of urea/amide (U/A) and urea/carbamate (U/C) units are reported. Structural studies at atomic resolution reveal hydrogen‐bonded helical structures akin to that formed by cognate Un homooligomers.
ISSN:	1433-7851 0044-8249 1521-3773 1521-3757
DOI:	10.1002/anie.201209838