Purification and Fibrillation of Recombinant Human Amyloid-β, Prion Protein, and Tau Under Native Conditions

  • Alexander Sandberg
  • Sofie Nyström
Part of the Methods in Molecular Biology book series (MIMB, volume 1779)


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 words

Amyloid Aβ Tau Prion protein Recombinant Purification Fibrillation Neurodegenerative disease 



This work was supported by the Swedish Alzheimer Foundation and The Swedish Research Council.


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© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Chemistry, IFM-Department of Physics, Chemistry and BiologyLinköping UniversityLinköpingSweden

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