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

作者: Longgang Jia , Wenping Zhao , Wei Wei , Xiao Guo , Wenjuan Wang

DOI: 10.1080/07388551.2020.1742646

关键词: Tau proteinα synucleinAmyloid βPurification methodsNeurotoxicityBiochemistryEscherichia coliRecombinant DNAAmyloidChemistry

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

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