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Updated: Aug 6, 2026
09:34
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
Programmable short peptide condensates with intrinsic enzyme-like activity
Hao Han1, Siyu Song2, Xi Gong1
1College of Polymer Science and Engineering, National Key Laboratory of Advanced Polymer Materials, Sichuan University, Chengdu, 610065, P. R. China. caoshoupeng@scu.edu.cn.
Journal of Materials Chemistry. B
|July 21, 2026
Summary
Researchers created programmable peptide coacervates with built-in enzyme-like activity. These biomimetic materials enhance reaction efficiency by concentrating substrates within compartments, offering a new platform for synthetic biology applications.
Area of Science:
- Biomaterials Science
- Synthetic Biology
- Chemical Engineering
Background:
- Biomolecular condensates are essential for cellular functions, orchestrating biochemical reactions.
- Synthetic analogues often rely on liquid-liquid phase separation (LLPS) for molecular confinement and reaction enhancement.
- Engineering inherent catalytic functionality into coacervate compartments remains a significant challenge.
Purpose of the Study:
- To develop programmable peptide-based coacervates with inherent enzyme-like catalytic activity.
- To engineer coacervate compartments capable of displaying catalytic functionality.
- To provide a versatile platform for programming LLPS behavior and constructing biomimetic active materials.
Main Methods:
- Co-assembly of short histidine-tagged peptides with triphenylalanine-based peptides.
- Formation of stable coacervate phases through cooperative assembly.
- Investigation of selective partitioning and sequestration of hydrophobic substrates within coacervates.
Main Results:
- Mixing specific peptide components led to stable coacervate formation, unlike rigid aggregates from individual components.
- The resulting peptide coacervates demonstrated inherent enzyme-like catalytic activity.
- Selective partitioning and sequestration of hydrophobic substrates enhanced local substrate concentration, promoting catalytic hydrolysis.
Conclusions:
- Catalytic activity can be directly encoded into coacervate-forming building blocks via rational peptide design.
- This approach provides a versatile platform for programming liquid-liquid phase separation behavior.
- The developed peptide coacervates serve as biomimetic active materials with potential synthetic biology applications.
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