Expression and purification of amyloid β-protein, tau, and α-synuclein in Escherichia coli: a review. (18th May 2020)

• Record Type: Journal Article
• Authors: Jia, Longgang; Zhao, Wenping; Wei, Wei; Guo, Xiao; Wang, Wenjuan; Wang, Ying; Sang, Jingcheng; Lu, Fuping; Liu, Fufeng
• Is Part Of: Critical reviews in biotechnology. Volume 40:Number 4(2020)
• Page Start: 475
• Page End: 489
• Publication Date: 2020-05-18
• Subjects: Protein conformational disease -- amyloid protein -- heterogenous protein expression -- purification -- E. coli expression system; Biotechnology -- Periodicals; Biotechnology -- Periodicals; Review Literature -- Periodicals; Public Health -- Periodicals; Environment -- Periodicals; Industry -- Periodicals; Biotechnology; Review Literature; Public Health; Environment; Industry; 660.6
• DOI: 10.1080/07388551.2020.1742646
• Languages: English
• ISSNs: 0738-8551

Abstract

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.