title: Atomic force microscopy study of human amylin (20-29) fibrils.
abstract: Here we present atomic force microscopy images of the fibrils formed by human amylin(20-29). This peptide is a fragment of the polypeptide amylin, the major proteinaceous component of amyloid deposits found in cases of type-II diabetes mellitus. Our results demonstrate that the amylin(20-29) peptide fragment forms amyloid-like fibrils that display polymorphic structures. Twisting along the axis of fibrils was often observed in fibrils aged for 6 hours but disappeared in mature fibrils aged for longer time periods.
authors.affiliation: Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham. NG7 2RD UK.
authors.forename: Victoria L
authors.initials: VL
authors.lastname: Sedman
authors.forename: Stephanie
authors.initials: S
authors.lastname: Allen
authors.forename: Weng C
authors.initials: WC
authors.lastname: Chan
authors.forename: Martyn C
authors.initials: MC
authors.lastname: Davies
authors.forename: Clive J
authors.initials: CJ
authors.lastname: Roberts
authors.forename: Saul J B
authors.initials: SJ
authors.lastname: Tendler
authors.forename: Philip M
authors.initials: PM
authors.lastname: Williams
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure*; D006801:Humans; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000648:ultrastructure*; D013997:Time Factors
chemical_list: D000682:Amyloid; D010446:Peptide Fragments; C117453:amylin (20-29)