ArticleNature communications2025
Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.
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 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Inhibition and Formation of Amyloid Fibrils in the Bulk and at the Interface of Biomolecular Condensates.Angewandte Chemie (International ed. in English) · 2026Review
- Quality by Design to Mitigate Aggregation: Mechanistic Insights and Analytical Strategies for Biopharmaceutical Manufacturing.Therapeutic innovation & regulatory science · 2026Review
- De novo design of peptides localizing at the interface of biomolecular condensates.Nature communications · 2026Article
- Controlling Multiphase Coacervate Wetting and Self-Organization by Interfacial Proteins.Journal of the American Chemical Society · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
Aggregation of amyloidogenic proteins is linked to age-related diseases. The presence of interfaces can affect their aggregation mechanism, often speeding up aggregation. α-Synuclein (αSyn) can adsorb to biomolecular condensates, leading to heterogenous nucleation and faster aggregation. Understanding the mechanism underlying localization of amyloidogenic proteins at condensate interfaces is crucial for developing strategies to prevent or reverse their binding. We show that αSyn localization to the surface of peptide-based heterotypic condensates is an adsorption process governed by the protein's condensate-amphiphilic nature, and the condensate surface charge. Adsorption occurs reversibly in multiple layers and plateaus at micromolar concentrations. Based on these findings, we rationally design three strategies to modulate αSyn accumulation: (i) addition of biomolecules that decrease the condensate ζ-potential, such as NTPs and RNA, (ii) competitive adsorption of proteins targeting the condensate interface, such as G3BP1, DDX4-YFP, EGFP-NPM1, Hsp70, Hsc70, and (iii) preferential adsorption of αSyn to membranes. Removing αSyn from the condensate interface slows aggregation, highlighting potential cellular control over protein adsorption and implications for therapeutic strategies.
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Registered trials
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