Fiber diffraction data indicate a hollow core for the Alzheimer's aβ 3-fold symmetric fibril.

McDonald M, Box H, Bian W, Kendall A, Tycko R, Stubbs G
J Mol Biol. 2012 423 (3): 454-61

PMID: 22903058 · PMCID: PMC3462308 · DOI:10.1016/j.jmb.2012.08.004

Amyloid β protein (Aβ), the principal component of the extracellular plaques found in the brains of patients with Alzheimer's disease, forms fibrils well suited to structural study by X-ray fiber diffraction. Fiber diffraction patterns from the 40-residue form Aβ(1-40) confirm a number of features of a 3-fold symmetric Aβ model from solid-state NMR (ssNMR) but suggest that the fibrils have a hollow core not present in the original ssNMR models. Diffraction patterns calculated from a revised 3-fold hollow model with a more regular β-sheet structure are in much better agreement with the observed diffraction data than patterns calculated from the original ssNMR model. Refinement of a hollow-core model against ssNMR data led to a revised ssNMR model, similar to the fiber diffraction model.

Copyright © 2012 Elsevier Ltd. All rights reserved.

MeSH Terms (9)

Alzheimer Disease Amyloid beta-Peptides Humans Models, Molecular Nuclear Magnetic Resonance, Biomolecular Peptide Fragments Plaque, Amyloid Protein Conformation X-Ray Diffraction

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