ArticleJournal of the American Chemical Society2024
Cell-Free Nonequilibrium Assembly for Hierarchical Protein/Peptide Nanopillars.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- ATP-fueled autonomous pathway-selective signal transduction on DNA-nanostructure tracks.Nature communications · 2026Article
- Features and mechanism of localized enzyme-assisted self-assembly of peptides from unilamellar vesicles.Frontiers in chemistry · 2026Article
- Enzyme-Instructed Self-Assembly for Cellular Supramolecular Chemistry.Chemistry, an Asian journal · 2025Review
- Balancing Chemical and Supramolecular Stability in OEGylated Supramolecular Polymers for Systemic Drug Delivery.Journal of the American Chemical Society · 2025Article
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
Cells contain intricate protein nanostructures, but replicating them outside of cells presents challenges. One such example is the vertical fibronectin pillars observed in embryos. Here, we demonstrate the creation of cell-free vertical fibronectin pillar mimics using nonequilibrium self-assembly. Our approach utilizes enzyme-responsive phosphopeptides that assemble into nanotubes. Enzyme action triggers shape changes in peptide assemblies, driving the vertical growth of protein nanopillars into bundles. These bundles, with peptide nanotubes serving as a template to remodel fibronectin, can then recruit collagen, which forms aggregates or bundles depending on their types. Nanopillar formation relies on enzyme-catalyzed nonequilibrium self-assembly and is governed by the concentrations of enzyme, protein, peptide, the structure of the peptide, and peptide assembly morphologies. Cryo-EM reveals unexpected nanotube thinning and packing after dephosphorylation, indicating a complex sculpting process during assembly. Our study demonstrates a cell-free method for constructing intricate, multiprotein nanostructures with directionality and composition.
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Registered trials
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