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Biochem Biophys Res Commun. 2012 Nov 30;428(4):458-62. doi: 10.1016/j.bbrc.2012.10.096. Epub 2012 Nov 3.

Solid-state NMR analysis of the β-strand orientation of the protofibrils of amyloid β-protein.

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  • 1Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.

Abstract

Alzheimer's disease (AD) is caused by abnormal deposition (fibrillation) of a 42-residue amyloid β-protein (Aβ42) in the brain. During the process of fibrillation, the Aβ42 takes the form of protofibrils with strong neurotoxicity, and is thus believed to play a crucial role in the pathogenesis of AD. To elucidate the supramolecular structure of the Aβ42 protofibrils, the intermolecular proximity of the Ala-21 residues in the Aβ42 protofibrils was analyzed by (13)C-(13)C rotational resonance experiments in the solid state. Unlike the Aβ42 fibrils, an intermolecular (13)C-(13)C correlation was not found in the Aβ42 protofibrils. This result suggests that the β-strands of the Aβ42 protofibrils are not in an in-register parallel orientation. Aβ42 monomers would assemble to form protofibrils with the β-strand conformation, then transform into fibrils by forming intermolecular parallel β-sheets.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID:
23131555
[PubMed - indexed for MEDLINE]
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