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.

中文翻译：

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淀粉样蛋白β蛋白，tau和α-突触核蛋白在大肠杆菌中的表达和纯化：综述。

淀粉样蛋白原蛋白的错误折叠和积累成各种形式的聚集中间体和不溶性淀粉样蛋白原纤维与50多种人类疾病有关。为了更好地探测其聚集和神经毒性，需要大量高质量的淀粉样蛋白。由于它们固有的疏水性，以高产率和高纯度获得淀粉样蛋白是一个挑战，它们引起了世界各地研究人员的关注。生物工程技术的飞速发展为获得大量重组淀粉样蛋白提供了技术支持。这篇综述讨论了三种淀粉样蛋白在微生物表达系统（尤其是大肠杆菌）中的可用表达和纯化方法，包括淀粉样蛋白β-蛋白，tau和α-突触核蛋白。并讨论了这些方法的优缺点。重要的是，这些方案也可用于其他疏水蛋白的表达和纯化。