Purification and Fibrillation of Recombinant Human Amyloid-β, Prion Protein, and Tau Under Native Conditions
Protein misfolding, aggregation, and amyloid formation is involved in a large number of diseases. Recombinantly expressed proteins to study the amyloid fibril formation process are important for mechanistic studies. We here report protocols for production, purification, and fibrillation of three different proteins commonly found in cerebral amyloid; Aβ and Tau found in Alzheimer’s disease, Chronic traumatic brain injury, Corticobasal degeneration, and Progressive Supranuclear Palsy and human prion protein found in Creutzfeldt-Jakob’s disease. The three protocols have in common that the protein is in a pH-neutral phosphate saline buffer during fibrillation to mimic their endogenous near physiological environment.
Key wordsAmyloid Aβ Tau Prion protein Recombinant Purification Fibrillation Neurodegenerative disease
This work was supported by the Swedish Alzheimer Foundation and The Swedish Research Council.