ArticleNature communications2025
Emergent mechanics of a networked multivalent protein condensate.
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 8 papers.
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Who cites it
8 citing papers in PubMed.
- Lipid-Mediated DNA-Protein Coupling Reinforces the Mechanics of HP1α-DNA Condensates.Small science · 2026Article
- Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026Article
- Computational rheometry for modeling viscoelasticity and mechanical responses of biomolecular condensates.Biophysical journal · 2026Article
- Differential effects of α-Synuclein monomers and seeds on the material properties of Tau condensates.bioRxiv : the preprint server for biology · 2026Article
- Tuning the state: Matching condensate material properties with physiological demands and pathological dysfunction.Cell insight · 2026Review
- Tuning mechanical softness as a design principle in drug delivery: A biomechanical perspective.Acta pharmaceutica Sinica. B · 2026Review
- From biomolecular condensates to functional nanomaterials: LLPS-inspired frameworks for nanoscale hydrogels and adaptive materials.Journal of nanobiotechnology · 2026Review
- Computational rheometry of viscoelastic networks: From random graphs to biomolecular condensates.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Multivalent proteins can form membraneless condensates in cells by liquid-liquid phase separation, and significant efforts have been made to study their biochemical properties. Here, we demonstrate the emergent mechanics of a functional multivalent condensate reconstituted with six postsynaptic density proteins, using atomic-force-microscopy-based mesoscale rheology and quantitative fluorescence measurements. The measured relaxation modulus and protein mobility reveal that the majority (80%) of the proteins in the condensate are mobile and diffuse through a dynamically cross-linked network made of the remaining (20%) non-mobile scaffold proteins. This percolating structure gives rise to a two-mode mechanical relaxation with an initial exponential decay followed by a long-time power-law decay, which differs significantly from simple Maxwell fluids. The power-law rheology with an exponent α ≃ 0.5 is a hallmark of weak bonds' binding/unbinding dynamics in the multivalent protein network. The concurrent molecular and mechanical profiling thus provides a reliable readout for characterizing the mechanical state of protein condensates and investigating their physiological functions and associations with diseases.
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Registered trials
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