Abstract
A growing body of evidence supports the nucleation hypothesis of fibrillar amyloid formation. In this article, it is hypothesized that the fibrils formed with human Aβ, rodent Aβ, and a mixture of the two peptides may form nearly identical physical structures with clearly different biological activities. Data is reported supporting the concept that a specific “strain” of nucleation seed could impart a new structure on a growing amyloid fibril, thereby changing its biological activity. The data that the biological activities of specific prion strains have a basis in strain-specific structure have been supported experimentally.
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Vitek, M.P. Radical changes in β-amyloid form and function. Molecular and Chemical Neuropathology 28, 49–55 (1996). https://doi.org/10.1007/BF02815204
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DOI: https://doi.org/10.1007/BF02815204