High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
14 01 2020
14 01 2020
Historique:
received:
12
10
2019
accepted:
18
12
2019
entrez:
16
1
2020
pubmed:
16
1
2020
medline:
11
11
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31937841
doi: 10.1038/s41598-019-57143-x
pii: 10.1038/s41598-019-57143-x
pmc: PMC6959368
doi:
Substances chimiques
Amyloid beta-Peptides
0
Fibroins
9007-76-5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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