β-strand mimetic foldamers rigidified through dipolar repulsion

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

Research output: Contribution to journalArticle

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 (US)
Pages (from-to)2649-2652
Number of pages4
JournalAngewandte Chemie - International Edition
Volume54
Issue number9
DOIs
StatePublished - Feb 23 2015

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Conformations
Proteins
Enthalpy

Keywords

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

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

β-strand mimetic foldamers rigidified through dipolar repulsion. / German, Elizabeth A.; Ross, Jonathan E.; Knipe, Peter C.; Don, Michaela F.; Thompson, Sam; Hamilton, Andrew.

In: Angewandte Chemie - International Edition, Vol. 54, No. 9, 23.02.2015, p. 2649-2652.

Research output: Contribution to journalArticle

German, Elizabeth A. ; Ross, Jonathan E. ; Knipe, Peter C. ; Don, Michaela F. ; Thompson, Sam ; Hamilton, Andrew. / β-strand mimetic foldamers rigidified through dipolar repulsion. In: Angewandte Chemie - International Edition. 2015 ; Vol. 54, No. 9. pp. 2649-2652.
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