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Biochim Biophys Acta. 2000 Jul 26;1502(1):16-30.

Alzheimer's amyloid fibrils: structure and assembly.

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  • 1Neurobiology Division, MRC Centre, Cambridge, UK. serpell@mrc-lmb.cam.ac.uk

Abstract

Structural studies of Alzheimer's amyloid fibrils have revealed information about the structure at different levels. The amyloid-beta peptide has been examined in various solvents and conditions and this has led to a model by which a conformational switching occurs from alpha-helix or random coil, to a beta-sheet structure. Amyloid fibril assembly proceeds by a nucleation dependent pathway leading to elongation of the fibrils. Along this pathway small oligomeric intermediates and short fibrillar structures (protofibrils) have been observed. In cross-section the fibril appears to be composed of several subfibrils or protofilaments. Each of these protofilaments is composed of beta-sheet structure in which hydrogen bonding occurs along the length of the fibre and the beta-strands run perpendicular to the fibre axis. This hierarchy of structure is discussed in this review.

PMID:
10899428
[PubMed - indexed for MEDLINE]
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