Sammanfattning

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.

Publicerad i

Scientific Reports
2020, Volym: 10, nummer: 1, artikelnummer: 235

SLU författare

• Rising, Anna

  • Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
    
  • Karolinska institutet

UKÄ forskningsämne

Biokemi och molekylärbiologi


Publikationens identifierare

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

Permanent länk till denna sida (URI)

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