ArticleACS applied bio materials2023
Silk Assembly against Hydrophobic Surfaces─Modeling and Imaging of Formation of Nanofibrils.
Article in ACS applied bio materials, 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
- Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Expanding the molecular grammar of polar residues and arginine in FUS phase separation.Nature chemical biology · 2025Article
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
- Genetic Functionalization of Protein-Based Biomaterials via Protein Fusions.Biomacromolecules · 2024Review
- Expanding the molecular grammar of polar residues and arginine in FUS prion-like domain phase separation and aggregation.bioRxiv : the preprint server for biology · 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
- Self-Assembly of RGD-Functionalized Recombinant Spider Silk Protein into Microspheres in Physiological Buffer and in the Presence of Hyaluronic Acid.ACS applied bio materials · 2023Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A detailed insight about the molecular organization behind spider silk assembly is valuable for the decoding of the unique properties of silk. The recombinant partial spider silk protein 4RepCT contains four poly-alanine/glycine-rich repeats followed by an amphiphilic C-terminal domain and has shown the capacity to self-assemble into fibrils on hydrophobic surfaces. We herein use molecular dynamic simulations to address the structure of 4RepCT and its different parts on hydrophobic versus hydrophilic surfaces. When 4RepCT is placed in a wing arrangement model and periodically repeated on a hydrophobic surface, β-sheet structures of the poly-alanine repeats are preserved, while the CT part is settled on top, presenting a fibril with a height of ∼7 nm and a width of ∼11 nm. Both atomic force microscopy and cryo-electron microscopy imaging support this model as a possible fibril formation on hydrophobic surfaces. These results contribute to the understanding of silk assembly and alignment mechanism onto hydrophobic surfaces.
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Registered trials
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