ArticleNature communications2022
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- Biomimetic peptide conjugates as emerging strategies for controlled release from protein-based materials.Drug delivery · 2025Review
- The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- The evolving role of solid state nuclear magnetic resonance methods in studies of amyloid fibrils.Current opinion in structural biology · 2025Review
- High-Strength, Antiswelling Directional Layered PVA/MXene Hydrogel for Wearable Devices and Underwater Sensing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Tuneable Recombinant Spider Silk Protein Hydrogels for Drug Release and 3D Cell Culture.Advanced functional materials · 2024Article
- Controlling Drug Partitioning in Individual Protein Condensates through Laser-Induced Microscale Phase Transitions.Journal of the American Chemical Society · 2024Article
- Effect of Phosphate on the Molecular Properties, Interactions, and Assembly of Engineered Spider Silk Proteins.Biomacromolecules · 2024Article
- Superfast Gelation of Spider Silk-Based Artificial Silk Protein.Gels (Basel, Switzerland) · 2024Article
- Natural and Engineered Isoforms of the Inflammasome Adaptor ASC Form Noncovalent, pH-Responsive Hydrogels.Biomacromolecules · 2023Article
- Advancing large-scale production of TEV protease through an innovative NT* tag-based fusion construct.Current research in structural biology · 2023Article
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Authors and funding
20 authors.
Funding
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Abstract
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.
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