ArticleProtein science : a publication of the Protein Society2023
Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- Fiber Reinforcement of Soft Spider Silk Hydrogels.Macromolecular rapid communications · 2026Article
- Structural and dynamic similarities of nanofibrils and microparticles of engineered spider silk proteins probed by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2026Article
- Wrinkling-Based Patterning and Recombinant Spider Silk-Based Coating Technologies - Toward Novel Applications.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Unraveling the Structure and Dynamics of Ac-PHF6-NHACS chemical neuroscience · 2024Article
- Only kosmotrope anions trigger fibrillization of the recombinant core spidroin eADF4(C16) from Araneus diadematus.Protein science : a publication of the Protein Society · 2023Article
- Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recombinant spider silk proteins can be prepared in scalable fermentation processes and have been proven as sources of biomaterials for biomedical and technical applications. Nanofibrils, formed through the self-assembly of these proteins, possess unique structural and mechanical properties, serving as fundamental building blocks for the fabrication of micro- and nanostructured scaffolds. Despite significant progress in utilizing nanofibrils-based morphologies of recombinant spider silk proteins, a comprehensive understanding of the molecular mechanisms of nanofibrils self-assembly remains a challenge. Here, a detailed kinetic study of nanofibril formation from a recombinant spider silk protein eADF4(C16) in dependence on the protein concentration, seeding, and temperature is provided. For the global fitting of kinetic data obtained during the fibril formation, we utilized the online platform AmyloFit. Evaluation of the data revealed that the self-assembly mechanism of recombinant spider silk is dominated by secondary nucleation. Thermodynamic analyses show that both primary and secondary nucleations, as well as the elongation step of the eADF4(C16), are endothermic processes.
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Registered trials
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