Controlling Helix Formation in the γ‐Peptide Superfamily: Heterogeneous Foldamers with Urea/Amide and Urea/Carbamate Backbones1. Issue 15 (4th March 2013)

• Record Type: Journal Article
• Authors: Pendem, Nagendar; Nelli, Yella Reddy; Douat, Céline; Fischer, Lucile; Laguerre, Michel; Ennifar, Eric; Kauffmann, Brice; Guichard, Gilles
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 15(2013)
• Page Start: 4147
• Page End: 4151
• Publication Date: 2013-03-04
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201209838
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>One fold to rule them all</bold>: 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 U_{<italic>n</italic>} homooligomers.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1x47f98q" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>