ArticleBiomacromolecules2021
Impact of Arginine-Phosphate Interactions on the Reentrant Condensation of Disordered Proteins.
Article in Biomacromolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Structural and functional divergence of cancer hotspot mutations in CREBBP.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Adenosine triphosphate as a modulator of protein interactions and stability.FEBS open bio · 2026Review
- Competition between protein-RNA clustering and phase separation drives re-entrant phase behavior of hnRNPA1.Nature communications · 2026Article
- Physicochemical Principles Governing the Intrinsically Disordered Salivary Peptide Histatin 5: Ensemble Structure, Electrostatics, and Environmental Responsiveness.The journal of physical chemistry. B · 2026Review
- Histone H3 tail charge patterns govern nucleosome condensate formation and dynamics.Nucleic acids research · 2026Article
- ATP and small amphiphilic molecules act as molecular matchmakers to fine-tune FET protein clusters.Communications chemistry · 2025Article
- ATP Can Act as a Stabilizer on Neutral Macromolecules.The journal of physical chemistry letters · 2025Article
- The Role of Counterions in the Assembly of Charged Virus-Like Shells.The journal of physical chemistry. B · 2025Article
- Selective Ion Binding and Uptake Shape the Microenvironment of Biomolecular Condensates.Journal of the American Chemical Society · 2025Article
- Histone H3 tail charge patterns govern nucleosome condensate formation and dynamics.bioRxiv : the preprint server for biology · 2025Article
- Article
- Reentrant Condensation of Polyelectrolytes Induced by Diluted Multivalent Salts: The Role of Electrostatic Gluonic Effects.Biomacromolecules · 2024Article
- Polymers for Disrupting Protein-Protein Interactions: Where Are We and Where Should We Be?Biomacromolecules · 2024Review
- Cellular Prion Protein Conformational Shift after Liquid-Liquid Phase Separation Regulated by a Polymeric Antagonist and Mutations.Journal of the American Chemical Society · 2024Article
- Reversible and size-controlled assembly of reflectin proteins using a charged azobenzene photoswitch.Chemical science · 2024Article
- Reentrant condensation of a multicomponent cola/milk system induced by polyphosphate.Food chemistry: X · 2024Article
- Unraveling the Microscopic Mechanism of Molecular Ion Interaction with Monoclonal Antibodies: Impact on Protein Aggregation.Molecular pharmaceutics · 2024Article
- Nonspecific Binding of Adenosine Tripolyphosphate and Tripolyphosphate Modulates the Phase Behavior of Lysozyme.Journal of the American Chemical Society · 2023Article
- Hydroxyapatite-Tethered Peptide Hydrogel Promotes Osteogenesis.Gels (Basel, Switzerland) · 2022Article
- Histone H3 and H4 tails play an important role in nucleosome phase separation.Biophysical chemistry · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Re-entrant condensation results in the formation of a condensed protein regime between two critical ion concentrations. The process is driven by neutralization and inversion of the protein charge by oppositely charged ions. Re-entrant condensation of cationic proteins by the polyvalent anions, pyrophosphate and tripolyphosphate, has previously been observed, but not for citrate, which has similar charge and size compared to the polyphosphates. Therefore, besides electrostatic interactions, other specific interactions between the polyphosphate ions and proteins must contribute. Here, we show that additional attractive interactions between arginine and tripolyphosphate determine the re-entrant condensation and decondensation boundaries of the cationic, intrinsically disordered saliva protein, histatin 5. Furthermore, we show by small-angle X-ray scattering (SAXS) that polyvalent anions cause compaction of histatin 5, as would be expected based solely on electrostatic interactions. Hence, we conclude that arginine-phosphate-specific interactions not only regulate solution properties but also influence the conformational ensemble of histatin 5, which is shown to vary with the number of arginine residues. Together, the results presented here provide further insight into an organizational mechanism that can be used to tune protein interactions in solution of both naturally occurring and synthetic proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.