ArticleNature communications2024
Active droplets through enzyme-free, dynamic phosphorylation.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed.
- Design of Fuel-Dependent, Complex-Coacervate-Based Synthetic Cells.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Bridging stimulus-responsive and dissipative peptide assemblies to build complex interactive biomaterials.Nature reviews. Chemistry · 2026Review
- Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.Journal of the American Chemical Society · 2026Article
- Enzyme-Free Phosphorylation with Kinetic Gating in a De Novo Coiled-Coil System.Journal of the American Chemical Society · 2026Article
- Chemically Fueled, Active Droplets Prevent the Aging of Peptides into Amyloid-Like Fibers.Journal of the American Chemical Society · 2025Article
- Sustained, Reversible, and Adaptive Non-Equilibrium Steady States of a Dissipative DNA-Based System.Angewandte Chemie (International ed. in English) · 2025Article
- Active droplets controlled by enzymatic reactions.Journal of the Royal Society, Interface · 2025Article
- Size control and oscillations of active droplets in synthetic cells.Nature communications · 2025Article
- Coacervate Droplets as Biomimetic Models for Designing Cell-Like Microreactors.Macromolecular rapid communications · 2024Review
- A Prebiotic Precursor to Life's Phosphate Transfer System with an ATP Analog and Histidyl Peptide Organocatalysts.Journal of the American Chemical Society · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Life continuously transduces energy to perform critical functions using energy stored in reactive molecules like ATP or NADH. ATP dynamically phosphorylates active sites on proteins and thereby regulates their function. Inspired by such machinery, regulating supramolecular functions using energy stored in reactive molecules has gained traction. Enzyme-free, synthetic systems that use dynamic phosphorylation to regulate supramolecular processes have not yet been reported, to our knowledge. Here, we show an enzyme-free reaction cycle that consumes the phosphorylating agent monoamidophosphate by transiently phosphorylating histidine and histidine-containing peptides. The phosphorylated species are labile and deactivate through hydrolysis. The cycle exhibits versatility and tunability, allowing for the dynamic phosphorylation of multiple precursors with a tunable half-life. Notably, we show the resulting phosphorylated products can regulate the peptide's phase separation, leading to active droplets that require the continuous conversion of fuel to sustain. The reaction cycle will be valuable as a model for biological phosphorylation but can also offer insights into protocell formation.
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Registered trials
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 OpenQuestion graph.