Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.

ABSTRACT: The aggregation of the prion protein (PrP) plays a key role in the development of prion diseases. In the past decade, a similar process has been associated with other proteins, such as Aβ, tau, and α-synuclein, which participate in other neurodegenerative diseases. It is increasingly recognized that the small oligomeric species of aggregates can play an important role in the development of prion diseases. However, determining the nature of the oligomers formed during the aggregation process has been experimentally difficult due to the lack of suitable methods capable of the detection and characterization of the low level of oligomers that may form. To address this problem, we have utilized single-aggregate methods to study the early events associated with aggregation of recombinant murine

SUBMITTER: Sang JC 

PROVIDER: S-EPMC6492631 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature