The mechanism of monomer transfer between two structurally distinct PrP oligomers.

ABSTRACT: In mammals, Prion pathology refers to a class of infectious neuropathologies whose mechanism is based on the self-perpetuation of structural information stored in the pathological conformer. The characterisation of the PrP folding landscape has revealed the existence of a plethora of pathways conducing to the formation of structurally different assemblies with different biological properties. However, the biochemical interconnection between these diverse assemblies remains unclear. The PrP oligomerisation process leads to the formation of neurotoxic and soluble assemblies called O1 oligomers with a high size heterodispersity. By combining the measurements in time of size distribution and average size with kinetic models and data assimilation, we revealed the existence of at least two struc

SUBMITTER: Armiento A 

PROVIDER: S-EPMC5528842 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature