title: Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22Δ) fibrils.
abstract: Alzheimer's disease (AD) is the most common form of dementia. Aggregation of amyloid β (Aβ), a peptide of 39-43 residues length, into insoluble fibrils is considered to initiate the disease. Determination of the molecular structure of Aβ fibrils is technically challenging and is a significant goal in AD research that may lead to design of effective therapeutical inhibitors of Aβ aggregation. Here, we present chemical-shift assignments for fibrils formed by highly pure recombinant Aβ1-40 with the Osaka E22Δ mutation that is found in familial AD. We show that that all regions of the peptide are rigid, including the N-terminal part often believed to be flexible in Aβ wt.
authors.affiliation: Laboratory of Physical Chemistry, ETH Zurich, Wolfgang Pauli Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Matthias
authors.initials: M
authors.lastname: Huber
authors.forename: Oxana Yu
authors.initials: OY
authors.lastname: Ovchinnikova
authors.forename: Anne K
authors.initials: AK
authors.lastname: Schütz
authors.forename: Rudi
authors.initials: R
authors.lastname: Glockshuber
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics*; D017433:Protein Structure, Secondary
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)