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

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

*Corresponding author for this work
1 Citation (Scopus)


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-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ 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 Aβ peptides per liter bacterial culture than previously reported.

Original languageEnglish
Article number235
JournalScientific Reports
Issue number1
Publication statusPublished - 01.12.2020

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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