Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation

Schutz, Anne K.; Wall, Joseph; Vagt, Toni; Huber, Matthias; Ovchinnikova, Oxana Y.; Cadalbert, Riccardo; Guntert, Peter; Bockmann, Anja; Glockshuber, Rudi; Meier, Beat H.

doi:10.1002/anie.201408598

Title: Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation

Journal Article · Wed Nov 12 23:00:00 EST 2014 · Angewandte Chemie (International Edition)

DOI: https://doi.org/10.1002/anie.201408598 · OSTI ID:1183283

Schutz, Anne K. ^[1]; Wall, Joseph ^[2]; Vagt, Toni ^[3]; Huber, Matthias ^[1]; Ovchinnikova, Oxana Y. ^[3]; Cadalbert, Riccardo ^[1]; Guntert, Peter ^[4]; Bockmann, Anja ^[5]; Glockshuber, Rudi ^[3]; Meier, Beat H. ^[1]

ETH Zurich, Wolfgang-Pauli-Strasse. Zurich (Switzerland)
Brookhaven National Lab. (BNL), Upton, NY (United States)
ETH Zurich, Zurich (Switzerland)
Goethe Univ., Frankfurt (Germany)
Univ. de Lyon, Lyon (France)

Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ 1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)

OSTI ID:: 1183283

Report Number(s):: BNL--107758-2015-JA; KP1501010

Journal Information:: Angewandte Chemie (International Edition), Journal Name: Angewandte Chemie (International Edition) Journal Issue: 1 Vol. 54; ISSN 1433-7851

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: English

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New Mechanism of Amyloid Fibril Formation Galzitskaya, Oxana Current Protein & Peptide Science, Vol. 20, Issue 6 https://doi.org/10.2174/1389203720666190125160937	journal	May 2019
The Role of Structural Polymorphism in Driving the Mechanical Performance of the Alzheimer's Beta Amyloid Fibrils Grasso, Gianvito; Rebella, Martina; Morbiducci, Umberto Frontiers in Bioengineering and Biotechnology, Vol. 7 https://doi.org/10.3389/fbioe.2019.00083	journal	April 2019
Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid β Assemblies Grasso, Gianvito; Rebella, Martina; Muscat, Stefano International Journal of Molecular Sciences, Vol. 19, Issue 2 https://doi.org/10.3390/ijms19020571	journal	February 2018
Different Synergy in Amyloids and Biologically Active Forms of Proteins Fabian, Piotr; Stapor, Katarzyna; Banach, Mateusz International Journal of Molecular Sciences, Vol. 20, Issue 18 https://doi.org/10.3390/ijms20184436	journal	September 2019
Alternative Structures of α-Synuclein Dułak, Dawid; Gadzała, Małgorzata; Banach, Mateusz Molecules, Vol. 25, Issue 3 https://doi.org/10.3390/molecules25030600	journal	January 2020
Mechanical and thermodynamic properties of Aβ ₄₂ , Aβ ₄₀ , and α-synuclein fibrils: a coarse-grained method to complement experimental studies Poma, Adolfo B.; Guzman, Horacio V.; Li, Mai Suan Beilstein Journal of Nanotechnology, Vol. 10 https://doi.org/10.3762/bjnano.10.51	journal	January 2019
Direct amide N-15 to C-13 transfers for solid-state assignment experiments in deuterated proteins Lends, Alons; Ravotti, Francesco; Zandomeneghi, Giorgia ETH Zurich https://doi.org/10.3929/ethz-b-000302186	text	January 2018
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy Guerrero-Ferreira, Ricardo; Taylor, Nicholas M. I.; Arteni, Ana-Andreea ETH Zurich https://doi.org/10.3929/ethz-b-000391777	text	January 2019
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy Guerrero-Ferreira, Ricardo; Taylor, Nicholas MI; Arteni, Ana-Andreea eLife, Vol. 8 https://doi.org/10.7554/elife.48907	journal	December 2019

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