How does domain replacement affect fibril formation of the rabbit/human prion proteins.

ABSTRACT:

Background

It is known that in vivo human prion protein (PrP) have the tendency to form fibril deposits and are associated with infectious fatal prion diseases, while the rabbit PrP does not readily form fibrils and is unlikely to cause prion diseases. Although we have previously demonstrated that amyloid fibrils formed by the rabbit PrP and the human PrP have different secondary structures and macromolecular crowding has different effects on fibril formation of the rabbit/human PrPs, we do not know which domains of PrPs cause such differences. In this study, we have constructed two PrP chimeras, rabbit chimera and human chimera, and investigated how domain replacement affects fibril formation of the rabbit/human PrPs.

Methodology/principal findings

As revealed by thioflavin

SUBMITTER: Yan X 

PROVIDER: S-EPMC4234653 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature