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- W2103172172 abstract "Amyloid-β peptide 1–42 (Aβ1–42), the predominant form in senile plaques, plays important roles in the pathogenesis of Alzheimer’s disease. Because Aβ1–42 has aggregation-prone nature, it has been difficult to produce in a soluble state in bacterial expression systems. In this study, we modified our expression system to increase the soluble fraction of Aβ1–42 in Escherichia coli (E. coli) cells. The expression level and solubility of recombinant Aβ1–42 induced at the low temperature (16 °C) is highly increased compared to that induced at 37 °C. To optimize expression temperature, the coding region of Aβ1–42 was constructed in a pCold vector, pCold–TF, which has a hexahistidine-tagged trigger factor (TF). Recombinant Aβ1–42 was expressed primarily as a soluble protein using pCold vector system and purified with a nickel-chelating resin. When the toxic effect of recombinant Aβ1–42 examined on human neuroblastoma SH-SY5Y cells, the purified Aβ1–42 induced cell toxicity on SH-SY5Y cells. In conclusion, the system developed in this study will provide a useful method for the production of aggregation prone-peptide such as Aβ1–42." @default.
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- W2103172172 date "2012-11-01" @default.
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- W2103172172 title "Large-scale production of soluble recombinant amyloid-β peptide 1–42 using cold-inducible expression system" @default.
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- W2103172172 doi "https://doi.org/10.1016/j.pep.2012.08.021" @default.
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