title: Helical-ribbon formation by a beta-amino acid modified amyloid beta-peptide fragment.
abstract: An addition to the family: The introduction of beta-amino acid residues into a modified amyloid beta peptide fragment resulted in well-defined helical nanoribbons (see cryo-TEM image) comprising beta strands mainly oriented perpendicular to the ribbon axis. The nanoribbons order into a flow-aligning nematic phase at higher concentration. The beta-strand nanoribbon structure is an addition to the known set of secondary structures adopted by beta-peptides.
authors.affiliation: Department of Chemistry, University of Reading, Whiteknights, Reading RG6 6AD, UK.
authors.forename: Valeria
authors.initials: V
authors.lastname: Castelletto
authors.forename: Ian W
authors.initials: IW
authors.lastname: Hamley
authors.forename: Rohan A
authors.initials: RA
authors.lastname: Hule
authors.forename: Darrin
authors.initials: D
authors.lastname: Pochan
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D046529:Microscopy, Electron, Transmission; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments