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

Author:

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,Biverstål Henrik

Abstract

AbstractDuring 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.

Funder

Magnus Bergvalls Stiftelse

Åhlén-stiftelsen

Stiftelsen för Gamla Tjänarinnor

Loo och Hans Ostermans Stiftelse för Medicinsk Forskning

Geriatric Diseases Foundation at Karolinska Institutet

INSTRUCT

Stiftelsen Olle Engkvist Byggmästare

Alzheimerfonden

Petrus och Augusta Hedlunds Stiftelse

Latvijas Zinatnes Padome

Norges Forskningsråd

EU Joint Programme - Neurodegenerative Disease Research

Center for innovative medicine (CIMED), Karolinska Insitutet

Vetenskapsrådet

Svenska Forskningsrådet Formas

VINNOVA

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

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