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Research article - Peer-reviewed, 2020

High-yield Production of Amyloid-beta Peptide Enabled by a Customized Spider Silk Domain

Abelein, Axel; Chen, Gefei; Kitoka, Kristīne; Aleksis, Rihards; Oleskovs, Filips; Sarr, Médoune; Landreh, Michael; Pahnke, Jens; Nordling, Kerstin; Kronqvist, Nina; Jaudzems, Kristaps; Rising, Anna; Johansson, Jan; Biverstal, Henrik


During storage in the silk gland, the N-terminal domain (NT) of spider silk proteins (spidroins) keeps the aggregation-prone repetitive region in solution at extreme concentrations. We observe that NTs from different spidroins have co-evolved with their respective repeat region, and now use an NT that is distantly related to previously used NTs, for efficient recombinant production of the amyloid-beta peptide (A beta) implicated in Alzheimer's disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of beta-hairpin repeat segments, gives exceptionally high yields of different human A beta variants as a solubility tag. This tool enables efficient production of target peptides also in minimal medium and gives up to 10 times more isotope-labeled monomeric A beta peptides per liter bacterial culture than previously reported.

Published in

Scientific Reports
2020, Volume: 10, number: 1, article number: 235

    UKÄ Subject classification

    Biochemistry and Molecular Biology

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