Method for folding of recombinant prion protein to soluble β-sheet secondary structure

Abstract

A key event in the pathogenesis of prion diseases is the change in structure of the normal cellular form of the prion protein from a predominantly α-helix form to the β-sheet-rich prion protein found in disease-associated tissue. To allow more detailed structural research into PrP misfolding, it is necessary to have techniques which enable enrichment of the β-sheet content in recombinant PrP. This method describes the procedure for inducing β-folding of recombinant PrP to resemble a disease-associated structure and ultimately produce soluble β-folded recombinant PrP.