Diphenylacetylene-linked peptide strands induce bidirectional β-sheet formation

Hannah Lingard, Jeongmin T. Han, Amber L. Thompson, Ivanhoe K.H. Leung, Richard T.W. Scott, Sam Thompson, Andrew D. Hamilton

Research output: Contribution to journalArticle

Abstract

In the search for synthetic mimics of protein secondary structures relevant to the mediation of protein-protein interactions, we have synthesized a series of tetrasubstituted diphenylacetylenes that display β-sheet structures in two directions. Extensive X-ray crystallographic and NMR solution phase studies are consistent with these proteomimetics adopting sheet structures, displaying both hydrophobic and hydrophilic amino acid side chains. The importance of β-sheet structures at the interface of protein-protein interactions has prompted the development of a range of synthetic strategies to template and stabilize this secondary structural motif. A tetrasubstituted diphenylacetylene is examined as a central nucleating point for the projection of extended sheet structures in two directions.

Original languageEnglish (US)
Pages (from-to)3650-3653
Number of pages4
JournalAngewandte Chemie - International Edition
Volume53
Issue number14
DOIs
StatePublished - Apr 1 2014

Keywords

  • beta-sheets
  • peptidomimetics
  • protein surfaces
  • protein-protein interactions
  • secondary structures

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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    Lingard, H., Han, J. T., Thompson, A. L., Leung, I. K. H., Scott, R. T. W., Thompson, S., & Hamilton, A. D. (2014). Diphenylacetylene-linked peptide strands induce bidirectional β-sheet formation. Angewandte Chemie - International Edition, 53(14), 3650-3653. https://doi.org/10.1002/anie.201309353