ArticleNature communications2024
Catalytic peptide-based coacervates for enhanced function through structural organization and substrate specificity.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
- Liquid-Liquid Phase Separation-Enhanced Multienzyme Catalysis: Mechanisms and Applications.ChemSusChem · 2026Review
- Programming Multidomain Peptides With Molecular Frustration Into Biomolecular Condensates.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Dynamic and Catalytic Multiphase Coacervates.Biomacromolecules · 2026Article
- Adaptive Coacervate Microreactors with Broad pH/Thermal Tolerance for Reaction Acceleration.JACS Au · 2026Article
- Diastereomeric Configuration Modulates Liquid-Liquid Phase Separation and Catalysis in Minimalist Dipeptide Coacervates.Angewandte Chemie (International ed. in English) · 2026Article
- MgChem & bio engineering · 2026Article
- Phase separation of a heterochiral peptide-drug conjugate amplified by ionic interactions.Nature communications · 2026Article
- Programmable Coacervates Based on Minimalist Sticker-Spacer Frameworks: Chemical Design, Functions, and Emerging Applications.ACS applied materials & interfaces · 2026Review
- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
- Structural and functional role of methylene linkers in self-coacervation-mediated membrane interaction and antiviral defense.Communications chemistry · 2026Article
- Metal-dependent and metal-free mechanisms of peptide condensate catalysts.Nature communications · 2026Article
- Sequence-Modulated Active Tripeptide Condensates for Tandem Catalysis.Angewandte Chemie (International ed. in English) · 2026Article
- Glycine Composition and Ion Valency Tune Phase Behavior and Drug Encapsulation in Designer Peptide Condensates.ACS applied materials & interfaces · 2026Article
- Competitive MgJACS Au · 2026Article
- From biomolecular condensates to functional nanomaterials: LLPS-inspired frameworks for nanoscale hydrogels and adaptive materials.Journal of nanobiotechnology · 2026Review
- Recent advances in coacervate protocells from passive catalysts to chemically programmable systems.Communications chemistry · 2026Review
- Surface Engineered Biomolecular Condensates for Targeted Cell Cytotoxicity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026Review
- Design and applications of synthetic biomolecular condensates.Nature nanotechnology · 2026Review
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Liquid-liquid phase separation (LLPS) in living cells provides innovative pathways for synthetic compartmentalized catalytic systems. While LLPS has been explored for enhancing enzyme catalysis, its potential application to catalytic peptides remains unexplored. Here, we demonstrate the use of coacervation, a key LLPS feature, to constrain the conformational flexibility of catalytic peptides, resulting in structured domains that enhance peptide catalysis. Using the flexible catalytic peptide P7 as a model, we induce reversible biomolecular coacervates with structured peptide domains proficient in hydrolyzing phosphate ester molecules and selectively sequestering phosphorylated proteins. Remarkably, these coacervate-based microreactors exhibit a 15,000-fold increase in catalytic efficiency compared to soluble peptides. Our findings highlight the potential of a single peptide to induce coacervate formation, selectively recruit substrates, and mediate catalysis, enabling a simple design for low-complexity, single peptide-based compartments with broad implications. Moreover, LLPS emerges as a fundamental mechanism in the evolution of chemical functions, effectively managing conformational heterogeneity in short peptides and providing valuable insights into the evolution of enzyme activity and catalysis in prebiotic chemistry.
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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.