ArticleNature communications2025
Size-controlled assembly of phase separated protein condensates with interfacial protein cages.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Advances in engineering and applications of synthetic phase-separated membraneless organelles in biotechnology.Synthetic and systems biotechnology · 2026Review
- Intrinsic Disorder as a Biomimetic Design Paradigm.Biomimetics (Basel, Switzerland) · 2026Article
- Protein oxidation in crowded environments.The Biochemical journal · 2026Review
- In-Situ Exploration of Phytic Acid-Mediated Supramolecular Self-Assembly and Gelation.Analytical chemistry · 2026Article
- Supersaturation, Nucleation, and Phase Separation of Mesoscopic Systems.Journal of the American Chemical Society · 2025Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.Nature communications · 2025Article
- Computational rheometry of viscoelastic networks: From random graphs to biomolecular condensates.bioRxiv : the preprint server for biology · 2025Article
- Polymeric and Polymer-Functionalized Drug Delivery Vectors: From Molecular Architecture and Elasticity to Cellular Uptake.Polymers · 2025Review
- Stabilization of Condensate Interfaces Using Dynamic Protein Insertion.Journal of the American Chemical Society · 2025Article
- The rheology and interfacial properties of biomolecular condensates.Biophysical reviews · 2025Review
- Nonviral protein cages as tools to decipher and combat viral threats.Npj viruses · 2025Review
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phase separation of specific proteins into liquid-like condensates is a key mechanism for forming membrane-less organelles, which organize diverse cellular processes in space and time. These protein condensates hold immense potential as biomaterials capable of containing specific sets of biomolecules with high densities and dynamic liquid properties. Despite their appeal, methods to manipulate protein condensate materials remain largely unexplored. Here, we present a one-pot assembly method to assemble coalescence-resistant protein condensates, ranging from a few μm to 100 nm in sizes, with surface-stabilizing protein cages. We discover that large protein cages (~30 nm), finely tuned to interact with condensates, efficiently localize on condensate surfaces and prevent the merging (coalescence) of condensates during phase separation. We precisely control condensate diameters by modulating condensate/cage ratios. In addition, the 3D structures of intact protein condensates with interfacial cages are visualized with cryo-electron tomography (ET). This work offers a versatile platform for designing size-controlled, surface-engineered protein condensate materials.
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