Journal
ACS CHEMICAL NEUROSCIENCE
Volume 5, Issue 5, Pages 340-345Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cn500019c
Keywords
Prion protein; Alzheimer's disease; A beta peptide; amyloid fibrils
Funding
- Spitz Brain Health Innovation Pilot Grant program
- National Institutes of Health [NS044158, NS074317]
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Recent studies indicate that the pathogenesis of Alzheimer disease may be related to the interaction between prion protein (PrP) and certain oligomeric species of A beta peptide. However, the mechanism of this interaction remains unclear and controversial. Here we provide direct experimental evidence that, in addition to previously demonstrated binding to A beta oligomers, PrP also interacts with mature A beta fibrils. However, contrary to the recent claim that PrP causes fragmentation of A beta fibrils into oligomeric species, no evidence for such a disassembly could be detected in the present study. In contrast, our data indicate that the addition of PrP to preformed A beta fibrils results in a lateral association of individual fibrils into larger bundles. These findings have potentially important implications for understanding the mechanism by which PrP might impact A beta toxicity as well as for the emerging efforts to use PrP-derived compounds as inhibitors of A beta-induced neurodegeneration. [GRAPHICS]
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