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β-Strand Mimetic Foldamers Rigidified through Dipolar Repulsion - Deleted

DOI: 10.1002/ange.201410290 DOI Help

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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