ArticleBiomacromolecules2021
Self-Assembly of Elastin-like Polypeptide Brushes on Silica Surfaces and Nanoparticles.
Article in Biomacromolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Technologies for engineering repetitive DNA.Quantitative biology (Beijing, China) · 2026Review
- Using cyclic voltammetry to probe the conformational transition of short elastin-like peptides.Communications chemistry · 2026Article
- Bioorthogonal Mussel-Inspired Elastin-like Nanocoatings for Indwelling Devices.ACS applied materials & interfaces · 2025Article
- The construction of elastin-like polypeptides and their applications in drug delivery system and tissue repair.Journal of nanobiotechnology · 2023Review
- Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Atomic Force Microscopy Imaging of Elastin Nanofibers Self-Assembly.Materials (Basel, Switzerland) · 2023Article
- Biomedical applications of solid-binding peptides and proteins.Materials today. Bio · 2023Review
- Design of Polypeptides Self-Assembling into Antifouling Coatings: Exploiting Multivalency.Biomacromolecules · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Control over the placement and activity of biomolecules on solid surfaces is a key challenge in bionanotechnology. While covalent approaches excel in performance, physical attachment approaches excel in ease of processing, which is equally important in many applications. We show how the precision of recombinant protein engineering can be harnessed to design and produce protein-based diblock polymers with a silica-binding and highly hydrophilic elastin-like domain that self-assembles on silica surfaces and nanoparticles to form stable polypeptide brushes that can be used as a scaffold for later biofunctionalization. From atomic force microscopy-based single-molecule force spectroscopy, we find that individual silica-binding peptides have high unbinding rates. Nevertheless, from quartz crystal microbalance measurements, we find that the self-assembled polypeptide brushes cannot easily be rinsed off. From atomic force microscopy imaging and bulk dynamic light scattering, we find that the binding to silica induces fibrillar self-assembly of the peptides. Hence, we conclude that the unexpected stability of these self-assembled polypeptide brushes is at least in part due to peptide-peptide interactions of the silica-binding blocks at the silica surface.
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Registered trials
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