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

Pendem Nagendar | Zendy; Nelli Yella Reddy | Zendy; Douat Céline | Zendy; Fischer Lucile | Zendy; Laguerre Michel | Zendy; Ennifar Eric | Zendy; Kauffmann Brice | Zendy; Guichard Gilles | Zendy

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

Author(s) -

Pendem Nagendar,

Nelli Yella Reddy,

Douat Céline,

Fischer Lucile,

Laguerre Michel,

Ennifar Eric,

Kauffmann Brice,

Guichard Gilles

Publication year - 2013

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201209838

Subject(s) - urea , chemistry , amide , carbamate , peptide , helix (gastropod) , stereochemistry , hydrogen bond , combinatorial chemistry , biochemistry , molecule , organic chemistry , biology , ecology , snail

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 U n homooligomers.

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