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β-Strand Mimetic Foldamers Rigidified through Dipolar Repulsion - Deleted
Authors:
Elizabeth A.
German
(University of Oxford)
,
Jonathan E.
Ross
(University of Oxford)
,
Peter
Knipe
(University of Oxford)
,
Michaela F.
Don
(University of Oxford)
,
Sam
Thompson
(University of Oxford)
,
Andrew D.
Hamilton
(University of Oxford)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Angewandte Chemie
, VOL 127 (9)
, PAGES 2687 - 2690
State:
Published (Approved)
Published:
February 2015
Diamond Proposal Number(s):
9981
Abstract: Many therapeutically relevant protein–protein interactions contain hot-spot regions on secondary structural elements, which contribute disproportionately to binding enthalpy. Mimicry of such α-helical regions has met with considerable success, however the analogous approach for the β-strand has received less attention. Presented herein is a foldamer for strand mimicry in which dipolar repulsion is a central determinant of conformation. Computation as well as solution- and solid-phase data are consistent with an ensemble weighted almost exclusively in favor of the desired conformation.
Journal Keywords: peptidomimetics; protein structures; protein-protein interactions; solid-state structures; synthetic methods
Subject Areas:
Biology and Bio-materials
Instruments:
I19-Small Molecule Single Crystal Diffraction
Added On:
15/03/2016 11:37
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