title: Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph.
abstract: The formation of fibrils of the amyloid-β (Aβ) peptide is considered to be a key event in the pathology of Alzheimer's disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular basis of AD. In this work, we present the sequential resonance assignment of one of the polymorphs of Aβ(1-42) fibrils. We show that most of the protein is rigid, while a stretch of 4 residues (11-14) is not visible by solid-state NMR spectroscopy due to dynamics.
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland.
authors.forename: Francesco
authors.initials: F
authors.lastname: Ravotti
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland.
authors.forename: Marielle Aulikki
authors.initials: MA
authors.lastname: Wälti
authors.affiliation: Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Max-von-Laue-Str. 9, 60438, Frankfurt am Main, Germany. guentert@em.uni-frankfurt.de.|Department of Chemistry, Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minami-Ohsawa, Hachioji, Tokyo, 192-0397, Japan. guentert@em.uni-frankfurt.de.
authors.forename: Peter
authors.initials: P
authors.lastname: Güntert
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland. roland.riek@phys.chem.ethz.ch.
authors.forename: Roland
authors.initials: R
authors.lastname: Riek
authors.affiliation: Institut de Biologie et Chemie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69007, Lyon, France. a.bockmann@ibcp.fr.
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland. beme@ethz.ch.
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry*; D000072757:Protein Conformation, beta-Strand; D055503:Protein Multimerization
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)
keywords: Alzheimer’s disease; Amyloid fibrils; Amyloid-β peptide; Solid-state NMR spectroscopy