title: Scanning tunnelling microscopy studies of beta-amyloid fibril structure and assembly.
abstract: Alzheimer's disease is in part characterised by the deposit of beta-amyloid peptide in the form of fibrils in the brain. In this study, the scanning tunnelling microscope (STM) has been used to provide high resolution images of synthetic fibril structure and formation as a function of time. Short fibrils are observed following brief peptide incubation times. At longer incubation periods ribbon like filaments were observed. These results suggest that beta-amyloid self-assembly is an ordered process, with a correlation between time of incubation and length of beta-amyloid filament growth.
authors.affiliation: Department of Pharmaceutical Sciences, University of Nottingham, UK.
authors.forename: A P
authors.initials: AP
authors.lastname: Shivji
authors.forename: F
authors.initials: F
authors.lastname: Brown
authors.forename: M C
authors.initials: MC
authors.lastname: Davies
authors.forename: K H
authors.initials: KH
authors.lastname: Jennings
authors.forename: C J
authors.initials: CJ
authors.lastname: Roberts
authors.lastname: Tendler SJf
authors.forename: M J
authors.initials: MJ
authors.lastname: Wilkinson
authors.forename: P M
authors.initials: PM
authors.lastname: Williams
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000096:biosynthesis* / Q000138:chemical synthesis / Q000737:chemistry / Q000648:ultrastructure*; D016252:Microscopy, Scanning Tunneling; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments