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Diphenylacetylene-Linked Peptide Strands Induce Bidirectional β-Sheet Formation

DOI: 10.1002/ange.201309353 DOI Help

Authors: Hannah Lingard (University of Oxford) , Jeongmin T. Han (University of Oxford) , Amber Thompson (University of Oxford) , Ivanhoe K. H. Leung (University of Oxford) , Richard T. W. Scott (University of Oxford) , Sam Thompson (University of Oxford) , Andrew Hamilton (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie , VOL 126 (14) , PAGES 3724 - 3727

State: Published (Approved)
Published: April 2014
Diamond Proposal Number(s): 7768

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 ?-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.

Journal Keywords: Beta-Faltblatt; Peptidmimetika; Proteinoberflächen; Protein-Protein-Wechselwirkungen; Sekundärstrukturen

Subject Areas: Chemistry

Instruments: I19-Small Molecule Single Crystal Diffraction

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