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High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain
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- Abelein, A (author)
- Karolinska Institutet
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- Chen, GF (author)
- Karolinska Institutet
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- Kitoka, K (author)
- Karolinska Institutet
- show more...
- Aleksis, R (author)
- Oleskovs, F (author)
- Pahnke, J (author)
- Jaudzems, K (author)
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- (creator_code:org_t)
- 2020-01-14
- 2020
- English.
- In: Scientific reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 10:1, s. 235-
- Journal article (peer-reviewed)
Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
- Abelein, A
- Chen, GF
- Kitoka, K
- Aleksis, R
- Oleskovs, F
- Sarr, M
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- Landreh, M
- Pahnke, J
- Nordling, K
- Kronqvist, N
- Jaudzems, K
- Rising, Anna
- Johansson, J
- Biverstal, H
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- Karolinska Institutet
- Swedish University of Agricultural Sciences
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