Expression and purification of amyloid β-protein, tau, and α-synuclein in Escherichia coli: a review

Abstract

Misfolding and accumulation of amyloidogenic proteins into various forms of aggregated intermediates and insoluble amyloid fibrils is associated with more than 50 human diseases. Large amounts of high-quality amyloid proteins are required for better probing of their aggregation and neurotoxicity. Due to their intrinsic hydrophobicity, it is a challenge to obtain amyloid proteins with high yield and purity, and they have attracted the attention of researchers from all over the world. The rapid development of bioengineering technology provides technical support for obtaining large amounts of recombinant amyloidogenic proteins. This review discusses the available expression and purification methods for three amyloid proteins including amyloid β-protein, tau, and α-synuclein in microbial expression systems, especially Escherichia coli, and discusses the advantages and disadvantages of these methods. Importantly, these protocols can also be referred to for the expression and purification of other hydrophobic proteins.

Keywords:

• Protein conformational disease
• amyloid protein
• heterogenous protein expression
• purification
• E. coli expression system

Disclosure statement

The authors report no conflict of interest.

Additional information

Funding

This work was funded by the National Key R&D Program (2018YFA0901700), the National Natural Science Foundation of China under Grants 21878234 and 21576199; the Natural Science Foundation of Tianjin of the Tianjin Municipal Science and Technology Commission under Grant 18JCZDJC33000.