A spider silk-derived solubility domain inhibits nuclear and cytosolic protein aggregation in human cells

Anna Katharina Schellhaus; Shanshan Xu; Maria E. Gierisch; Julia Vornberger; Jan Johansson; Nico P. Dantuma

doi:10.1038/s42003-022-03442-5

Communications Biology (May 2022)

A spider silk-derived solubility domain inhibits nuclear and cytosolic protein aggregation in human cells

Anna Katharina Schellhaus,
Shanshan Xu,
Maria E. Gierisch,
Julia Vornberger,
Jan Johansson,
Nico P. Dantuma

Affiliations

Anna Katharina Schellhaus: Department of Cell and Molecular Biology, Karolinska Institutet
Shanshan Xu: Department of Cell and Molecular Biology, Karolinska Institutet
Maria E. Gierisch: Department of Cell and Molecular Biology, Karolinska Institutet
Julia Vornberger: Department of Cell and Molecular Biology, Karolinska Institutet
Jan Johansson: Department of Biosciences and Nutrition, Karolinska Institutet, Neo
Nico P. Dantuma: Department of Cell and Molecular Biology, Karolinska Institutet

DOI: https://doi.org/10.1038/s42003-022-03442-5
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 8

Abstract

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Spider-silk protein increases the solubility of an aggregation-prone reporter protein, showing potential applications in controlling aggregation of disease-associated proteins by natural solubility domains.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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