The molecular basis of the prion model and the mechanistic models of the prion amplification are summarized. The infection is a conversion of the host encoded prion protein PrP from its cellular isoform PrP^C into a pathological and infectious isoform PrP^Sc. The conversion process was investigated by in vitro studies on recombinant PrP. Dimeric and oligomeric PrP conformations were identified as intermediate states. In particular, a monomer-dimer equilibrium of partially denatured PrP was described as the essential step preceding fibrillization. During the last years fibrils could be formed from recombinant PrP, and indeed these fibrils exhibited infecitivity; by these experiments the prion model can be regarded today as experimentally proven. Since in vivo PrP^C is presented on the outer surface of the cell membrane and has to be detached from the membrane during the conversion process, the interaction of PrP^C with raft like lipid membranes was studied by quantitative methods. PrP^C can form oligomers on the surface of the membrane. The thermodynamic and kinetic parameters are the basis of the so-called two-phase-model which takes into account the role of the cell membrane in the conversion process of PrP^C into PrP^Sc.

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