The prion pathology is based on autonomous structural information propagation towards single or multiple protein conformational changes. Since this last decade the prion concept referring to the transmission of structural information has been extended to several regulation systems and pathologies including Alzheimer and Parkinson’s diseases. The unified theory in Prion replication implies structural information transference from the prion to a non-prion conformer through a mechanism also called improperly, with regards to biophysical considerations “seeding” phenomenon. Recently we reported that prion replication is intrinsically source of structural diversification. The coexistence of multiple prion assemblies with different structural and replication propensity questions how they are maintained within the same media and how they escape to best replicator selection.
The analysis of the quaternary structure dynamic of prion assemblies revealed the existence of an exchange process within the structurally diverse prion assemblies. This exchange process has for consequence the apparition of dumped-oscillation. Data assimilation and kinetical modelling conduced us to propose a kinetical scheme in which structurally diverse prion assemblies catalytically exchange material. According to this kinetic scheme a catalytical depolymerization competes with a catalytic conformational change.