ArticleThe Journal of chemical physics2025
Intrinsic hydrophobicity of IDP-based biomolecular condensates drives their partial drying on membrane surfaces.
Article in The Journal of chemical physics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Liquid-Liquid Phase Separation-Enhanced Multienzyme Catalysis: Mechanisms and Applications.ChemSusChem · 2026Review
- Chain collapse, reduced dielectric, and water release drive protein phase separation.Biophysical journal · 2026Article
- Fluorescence-based mapping of condensate dielectric permittivity uncovers hydrophobicity-driven membrane interactions.Nature communications · 2026Article
- Backbone-mediated weakening of pairwise interactions enables percolation in peptide-based mimics of protein condensates.Communications chemistry · 2025Article
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3 authors.
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Abstract
The localization of biomolecular condensates to intracellular membrane surfaces has emerged as an important feature of sub-cellular organization. In this work, we study the wetting behavior of biomolecular condensates on various substrates. We use confocal microscopy to measure the contact angles of model condensates formed by intrinsically disordered protein Ddx4N. We show the importance of taking optical aberrations into account, as these impact apparent contact angle measurements. Ddx4N condensates are seen to partially dry (contact angles above 90°) a model membrane, with little dependence on the magnitude of charge on, or tyrosine content of, Ddx4N. Further contact angle measurements on surfaces of varying hydrophilicity reveal a preference of Ddx4N condensates for hydrophobic surfaces, suggesting an intrinsic repulsion between protein condensates and hydrophilic membrane surfaces. This observation is in line with previous studies relating protein adsorption to surface hydrophilicity. Our work advances the understanding of the molecular details governing the localization of biomolecular condensates.
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