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Interaction between prion protein and A? amyloid fibrils revisited.


ABSTRACT: 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? 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? oligomers, PrP also interacts with mature A? fibrils. However, contrary to the recent claim that PrP causes fragmentation of A? 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? 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? toxicity as well as for the emerging efforts to use PrP-derived compounds as inhibitors of A?-induced neurodegeneration.

SUBMITTER: Nieznanski K 

PROVIDER: S-EPMC4030797 | biostudies-other | 2014 May

REPOSITORIES: biostudies-other

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Interaction between prion protein and Aβ amyloid fibrils revisited.

Nieznanski Krzysztof K   Surewicz Krystyna K   Chen Shugui S   Nieznanska Hanna H   Surewicz Witold K WK  

ACS chemical neuroscience 20140401 5


Recent studies indicate that the pathogenesis of Alzheimer disease may be related to the interaction between prion protein (PrP) and certain oligomeric species of Aβ 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 Aβ oligomers, PrP also interacts with mature Aβ fibrils. However, contrary to the recent claim that PrP causes fragmentation of Aβ fibrils into ol  ...[more]

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