ArticleBiomacromolecules2025
Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related α-Synuclein.
Article in Biomacromolecules, 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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Who cites it
4 citing papers in PubMed.
- Phase separation in neurodegenerative disorders: a metabolic perspective on protein aggregation and therapeutic targeting.Translational neurodegeneration · 2026Review
- α-Synuclein aggregation landscape from phase separation to neurotoxic intermediates.FEBS letters · 2026Review
- Lung microbiota-derived deoxyinosine alleviates TBI-aggravated sepsis-induced lung injury via the S100A9/RAGE pathway.Journal of neuroinflammation · 2026Article
- Tau Enhances Aggregation of S100A9 Protein and Further Association of Its Fibrils.International journal of molecular sciences · 2025Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Liquid-liquid phase separation of proteins and nucleic acids is a rapidly emerging field of study, aimed at understanding the process of biomolecular condensate formation. Recently, it has been discovered that different neurodegenerative disease-related proteins, such as α-synuclein and amyloid-β are capable of forming heterotypic droplets. Other reports have also shown non-LLPS cross-interactions between various amyloidogenic proteins and the resulting influence on their amyloid fibril formation. This includes the new discovery of pro-inflammatory S100A9 affecting the aggregation of both amyloid-β, as well as α-synuclein. In this study, we explore the formation of heterotypic droplets by S100A9 and α-synuclein. We show that their mixture is capable of assembling into both homotypic and heterotypic condensates and that this cross-interaction alters the aggregation mechanism of α-synuclein. These results provide insight into the influence of S100A9 on the process of neurodegenerative disease-related protein LLPS and aggregation.
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