title: New cylindrical peptide assemblies defined by extended parallel β-sheets.
abstract: A new approach to non-covalent peptide-based nanotubular or rod-like structures is presented, whereby the monomeric units are preorganised into a β-strand geometry that templates the formation of an extended and unusual parallel β-sheet rod-like structure. The conformational constraint is introduced by Huisgen cycloaddition to give a triazole-based macrocycle, with the resulting self-assembled structures stabilized by a well-defined series of intermolecular hydrogen bonds.
authors.affiliation: School of Chemistry and Physics, The University of Adelaide, North Terrace, Adelaide SA 5005, Australia.
authors.forename: Ashok D
authors.initials: AD
authors.lastname: Pehere
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Sumby
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Abell
mesh_terms: D008958:Models, Molecular; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D017433:Protein Structure, Secondary
chemical_list: D009842:Oligopeptides