Abstract
Fibrillar aggregates of Aβ peptides and tau protein are defining features of Alzheimer's disease (AD) and evidence is accumulating that peptide conformation within fibrils correlates with disease subtype. Nevertheless, high resolution structures of fibrillar polymorphs fall short of defining the molecular mechanisms underlying disease. Mapping of the spatial distribution of polymorphs at multiple length scales—within plaques and tangles, across brain tissue, and in multiple brain regions—is being carried out to supplement high resolution information.
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