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Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue.

Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R
Cell 154 1257-68 (2013)
Cited: 599 times
EuropePMC logo PMID: 24034249

Abstract

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here, we investigate structures of human brain-derived Aβ fibrils, using seeded fibril growth from brain extract and data from solid-state nuclear magnetic resonance and electron microscopy. Experiments on tissue from two Alzheimer's disease (AD) patients with distinct clinical histories showed a single predominant 40 residue Aβ (Aβ40) fibril structure in each patient; however, the structures were different from one another. A molecular structural model developed for Aβ40 fibrils from one patient reveals features that distinguish in-vivo- from in-vitro-produced fibrils. The data suggest that fibrils in the brain may spread from a single nucleation site, that structural variations may correlate with variations in AD, and that structure-specific amyloid imaging agents may be an important future goal.

Reviews - 2m4j mentioned but not cited (19)

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Articles - 2m4j mentioned but not cited (46)

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