β-Strand mimetic foldamers rigidified through dipolar repulsion

Elizabeth A. German, Jonathan E. Ross, Peter C. Knipe, Michaela F. Don, Sam Thompson*, Andrew D. Hamilton

*Corresponding author for this work

Research output: Contribution to journalArticle

23 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2649-2652
Number of pages4
JournalAngewandte Chemie International Edition
Volume54
Issue number9
Early online date19 Jan 2015
DOIs
Publication statusPublished - 17 Feb 2015

Keywords

  • Peptidomimetics
  • Protein structures
  • Protein-protein interactions
  • Solid-state structures
  • Synthetic methods

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

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