Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 08 2022
15 08 2022
Historique:
received:
08
12
2021
accepted:
15
07
2022
entrez:
15
8
2022
pubmed:
16
8
2022
medline:
18
8
2022
Statut:
epublish
Résumé
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 °C. The gelation is caused by NT α-helix to β-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.
Identifiants
pubmed: 35970823
doi: 10.1038/s41467-022-32093-7
pii: 10.1038/s41467-022-32093-7
pmc: PMC9378615
doi:
Substances chimiques
Hydrogels
0
Recombinant Proteins
0
Silk
0
Fibroins
9007-76-5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4695Informations de copyright
© 2022. The Author(s).
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