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Research article - Peer-reviewed, 2022

Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

Arndt, Tina; Jaudzems, Kristaps; Shilkova, Olga; Francis, Juanita; Johansson, Mathias; Laity, Peter R.; Sahin, Cagla; Chatterjee, Urmimala; Kronqvist, Nina; Barajas-Ledesma, Edgar; Kumar, Rakesh; Chen, Gefei; Stromberg, Roger; Abelein, Axel; Langton, Maud; Landreh, Michael; Barth, Andreas; Holland, Chris; Johansson, Jan; Rising, Anna


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 degrees C which allows for ease of production and fusion protein modification to generate functional biomaterials.Recombinant spider silk proteins (spidroins) have multiple potential applications in development of novel biomaterials, but their multimodal and aggregation-prone nature have complicated production and straightforward applications. Here, we report that recombinant miniature spidroins, and importantly also the N-terminal domain (NT) on its own, rapidly form self-supporting and transparent hydrogels at 37 degrees C. The gelation is caused by NT alpha-helix to beta-sheet conversion and formation of amyloid-like fibrils, and fusion proteins composed of NT and green fluorescent protein or purine nucleoside phosphorylase form hydrogels with intact functions of the fusion moieties. Our findings demonstrate that recombinant NT and fusion proteins give high expression yields and bestow attractive properties to hydrogels, e.g., transparency, cross-linker free gelation and straightforward immobilization of active proteins at high density.

Published in

Nature Communications
2022, Volume: 13, number: 1, article number: 4695