Radical changes in beta-amyloid form and function.
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 A beta, rodent A beta, 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.
Vitek
M P
MP
Duke University Medical Center, Durham, NC 27710, USA.
D000544:Alzheimer Disease / Q000378:metabolism; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000502:physiology* / Q000633:toxicity; D000818:Animals; D017127:Glycation End Products, Advanced / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry; D017433:Protein Structure, Secondary; D012377:Rodentia; D017386:Sequence Homology, Amino Acid
D016229:Amyloid beta-Peptides; D017127:Glycation End Products, Advanced; D011328:Prions