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High yield production of amyloid-ß peptide enabled by a customized spider silk domain

Abelein, Axel and Chen, Gefei and Kitoka, Kristīne and Aleksis, Rihards and Oleskovs, Filips and Sarr, Médoune and Landreh, Michael and Pahnke, Jens and Nordling, Kerstin and Kronqvist, Nina and Jaudzems, Kristaps and Rising, Anna and Johansson, Jan and Biverstal, Henrik (2020). High yield production of amyloid-ß peptide enabled by a customized spider silk domain. Scientific Reports. 10 , 235 , 1-10
[Journal article]

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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 efcient recombinant production of the amyloid-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes fagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of diferent 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.

Authors/Creators:Abelein, Axel and Chen, Gefei and Kitoka, Kristīne and Aleksis, Rihards and Oleskovs, Filips and Sarr, Médoune and Landreh, Michael and Pahnke, Jens and Nordling, Kerstin and Kronqvist, Nina and Jaudzems, Kristaps and Rising, Anna and Johansson, Jan and Biverstal, Henrik
Title:High yield production of amyloid-ß peptide enabled by a customized spider silk domain
Year of publishing :2020
Volume:10
Article number:235
Number of Pages:10
Publisher:Springer Nature
ISSN:2045-2322
Language:English
Publication Type:Journal article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology
URN:NBN:urn:nbn:se:slu:epsilon-p-105883
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-105883
Additional ID:
Type of IDID
DOI10.1038/s41598-019-57143-x
ID Code:17154
Faculty:VH - Faculty of Veterinary Medicine and Animal Science
Department:(VH) > Dept. of Anatomy, Physiology and Biochemistry
Deposited By: SLUpub Connector
Deposited On:29 Jun 2020 07:18
Metadata Last Modified:29 Jun 2020 07:18

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