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Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

Colvin, Michael T ; Silvers, Robert ; Ni, Qing Zhe ; Can, Thach V ; Sergeyev, Ivan ; Rosay, Melanie ; Donovan, Kevin J ; Michael, Brian ; Wall, Joseph ; Linse, Sara ; Griffin, Robert G

Journal of the American Chemical Society, 03 August 2016, Vol.138(30), pp.9663-74 [Peer Reviewed Journal]

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  • Title:
    Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils
  • Author: Colvin, Michael T ; Silvers, Robert ; Ni, Qing Zhe ; Can, Thach V ; Sergeyev, Ivan ; Rosay, Melanie ; Donovan, Kevin J ; Michael, Brian ; Wall, Joseph ; Linse, Sara ; Griffin, Robert G
  • Description: Amyloid-β (Aβ) is a 39-42 residue protein produced by the cleavage of the amyloid precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that are a hallmark of Alzheimer's disease (AD). The most prominent forms of Aβ are Aβ1-40 and Aβ1-42, which differ by two amino acids (I and A) at the C-terminus. However, Aβ42 is more neurotoxic and essential to the etiology of AD. Here, we present an atomic resolution structure of a monomorphic form of AβM01-42 amyloid fibrils derived from over 500 (13)C-(13)C, (13)C-(15)N distance and backbone angle structural constraints obtained from high field magic angle spinning NMR spectra. The structure (PDB ID: 5KK3 ) shows that the fibril core consists of a dimer of Aβ42 molecules, each containing four β-strands in a S-shaped amyloid fold, and arranged in a manner that generates two hydrophobic cores that are capped at the end of the chain by a salt bridge. The outer surface of the monomers presents hydrophilic side chains to...
  • Is Part Of: Journal of the American Chemical Society, 03 August 2016, Vol.138(30), pp.9663-74
  • Identifier: E-ISSN: 1520-5126 ; PMID: 27355699 Version:1 ; DOI: 10.1021/jacs.6b05129
  • Subjects: Nuclear Magnetic Resonance, Biomolecular ; Protein Aggregates ; Amyloid Beta-Peptides -- Chemistry ; Peptide Fragments -- Chemistry
  • Language: English

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