Nature Communications (Aug 2022)
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform
- Tina Arndt,
- Kristaps Jaudzems,
- Olga Shilkova,
- Juanita Francis,
- Mathias Johansson,
- Peter R. Laity,
- Cagla Sahin,
- Urmimala Chatterjee,
- Nina Kronqvist,
- Edgar Barajas-Ledesma,
- Rakesh Kumar,
- Gefei Chen,
- Roger Strömberg,
- Axel Abelein,
- Maud Langton,
- Michael Landreh,
- Andreas Barth,
- Chris Holland,
- Jan Johansson,
- Anna Rising
Affiliations
- Tina Arndt
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Kristaps Jaudzems
- Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
- Olga Shilkova
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Juanita Francis
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Mathias Johansson
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
- Peter R. Laity
- Department of Materials Science and Engineering, The University of Sheffield
- Cagla Sahin
- Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet
- Urmimala Chatterjee
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Nina Kronqvist
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Edgar Barajas-Ledesma
- Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet
- Rakesh Kumar
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Gefei Chen
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Roger Strömberg
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Axel Abelein
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Maud Langton
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
- Michael Landreh
- Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet
- Andreas Barth
- Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University
- Chris Holland
- Department of Materials Science and Engineering, The University of Sheffield
- Jan Johansson
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- Anna Rising
- Department of Biosciences and Nutrition, Karolinska Institutet, Neo
- DOI
- https://doi.org/10.1038/s41467-022-32093-7
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 14
Abstract
Recombinant spider silks are of interest but the multimodal and aggregation-prone nature of them is a limitation. Here, the authors report on a miniature spidroin based on the N-terminal domain which forms a hydrogel at 37 °C which allows for ease of production and fusion protein modification to generate functional biomaterials.
