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Research article - Peer-reviewed, 2020

High yield production of amyloid-ß 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

Abstract

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

Authors' information

Abelein, Axel
Karolinska Institutet
Chen, Gefei
Karolinska Institute
Kitoka, Kristīne
Latvian Institute of Organic Synthesis
Aleksis, Rihards
Latvian Institute of Organic Synthesis
Oleskovs, Filips
Latvian Institute of Organic Synthesis
Sarr, Médoune
Karolinska Institute
Landreh, Michael
Karolinska Institute
Pahnke, Jens
University of Latvia
Nordling, Kerstin
Karolinska Institutet
Kronqvist, Nina
Karolinska Institute
Jaudzems, Kristaps
Latvian Institute of Organic Synthesis
Karolinska Institute
Swedish University of Agricultural Sciences, Department of Anatomy, Physiology and Biochemistry (AFB)
Johansson, Jan
Karolinska Institute
Biverstal, Henrik
Latvian Institute of Organic Synthesis

UKÄ Subject classification

Biochemistry and Molecular Biology

Publication Identifiers

DOI: https://doi.org/10.1038/s41598-019-57143-x

URI (permanent link to this page)

https://res.slu.se/id/publ/105883