ArticleJournal of the American Chemical Society2025
Stabilization of Condensate Interfaces Using Dynamic Protein Insertion.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- De novo design of peptides localizing at the interface of biomolecular condensates.Nature communications · 2026Article
- Dynamic Covalent Boronate Chemistry forJournal of the American Chemical Society · 2026Article
- Complex Coacervate Emulsions as a Strategy to Stabilize Enzymes for Catalysis in Organic Solvents.ACS macro letters · 2026Article
- Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.Nature communications · 2025Article
- Automated navigation of condensate phase behavior with active machine learning.Nature communications · 2025Article
- Dendritic Membranized Coacervate Microdroplets: A Robust Platform for Synthetic-Living Cell Consortia.Journal of the American Chemical Society · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coacervates have been widely used to mimic membraneless organelles (MLOs). However, coacervates without a membrane or stabilizing surface do not feature the same level of stability as MLOs. This study shows that specifically engineered surface-active proteins can interact with the interface of polypeptide coacervates, conferring resistance to coacervate dissolution and fusion. Modulating the molecular characteristics of these coacervate stabilizing proteins highlighted that their dimerization aids in achieving effective interface stabilizers. Cryo-TEM imaging showed a densely packed protein monolayer at the coacervate-liquid interface, while single-molecule super-resolution microscopy captured the dynamic nature of this protein layer, with the proteins rapidly (un)docking and moving across the coacervate interface within milliseconds. These findings suggest a dynamic form of coacervate stabilization driven by transient protein interactions at the condensate interface. This unique form of coacervate stabilization not only provides a new approach to developing stable and dynamically exchanging synthetic condensate systems but, as model systems, can also significantly contribute to our understanding of the mechanisms underlying the temporal stability of MLOs in nature.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.