title: Diphenylacetylene-linked peptide strands induce bidirectional β-sheet formation.
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.
authors.affiliation: Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) http://hamilton.chem.ox.ac.uk.
authors.forename: Hannah
authors.initials: H
authors.lastname: Lingard
authors.forename: Jeongmin T
authors.initials: JT
authors.lastname: Han
authors.forename: Amber L
authors.initials: AL
authors.lastname: Thompson
authors.forename: Ivanhoe K H
authors.initials: IK
authors.lastname: Leung
authors.forename: Richard T W
authors.initials: RT
authors.lastname: Scott
authors.forename: Sam
authors.initials: S
authors.lastname: Thompson
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Hamilton
mesh_terms: D000114:Acetylene / Q000031:analogs & derivatives* / Q000737:chemistry; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D010455:Peptides / Q000737:chemistry; D017510:Protein Folding; D058767:Protein Unfolding
chemical_list: D010455:Peptides; C044735:biphenylacetylene; D000114:Acetylene
keywords: beta-sheets; peptidomimetics; protein surfaces; protein-protein interactions; secondary structures