ArticleNature communications2025
Amino acids bind to phase-separating proteins and modulate biomolecular condensate stability and dynamics.
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.
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Who cites it
4 citing papers in PubMed.
- Seeing the Chemistry of Biomolecular Condensates: In Situ Mapping of Composition and Water Content.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Partition Coefficients Reveal Changes in Properties of Low-Contrast Biomolecular Condensates.bioRxiv : the preprint server for biology · 2026Article
- The Protonic Brain: Nanoscale pH Dynamics, Proton Wires, and Acid-Base Information Coding in Neural Tissue.International journal of molecular sciences · 2026Review
- RNA-Protein Assemblies: A Review of Biophysical Principles and Coarse-Grained Modeling Approaches.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
7 authors.
Funding
Abstract
Biomolecular condensates (BCs) are ubiquitous compartments that regulate key functions in cells. BCs are surrounded by a complex intracellular environment, of which amino acids (AAs) are prominent components. However, it is unclear how AAs interact with condensate components and influence the material properties of condensates. Here, we demonstrate that phase separation is suppressed with glycine by using model heterotypic condensates composed of nucleophosmin 1 and ribosomal ribonucleic acid. The condensate density decreases, and the dynamics within the condensate increase. We find that glycine weakly binds to amide groups in the protein backbone and aromatic groups in the side chains, weakening the backbone-backbone interactions between neutral and charged disordered proteins while strengthening the interactions between aromatic stickers. This leads to different modulations of the phase behaviour in condensates formed by π/cation-π interactions and charge complexation. We further show that a modulation effect on BCs is observed for other proteinogenic AAs and can be transferred to short homopeptides. These insights offer strategies to modulate the dynamic properties of BCs in vivo.
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