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Development of Dipeptide-Based Liquid Droplets and Fibrils as Enzyme-Mimics.
Sagar Jawla1, Mousumi Samanta1, V Haridas1,2
1Department of Chemistry, Indian Institute of Technology, Delhi, New Delhi, 110016, India.
Small (Weinheim an Der Bergstrasse, Germany)
|May 24, 2025
Summary
Researchers developed a simple dipeptide that self-assembles into coacervates, acting as microreactors. This minimalistic peptide also forms catalytic fibrils, mimicking esterase activity for synthetic biology applications.
Area of Science:
- Supramolecular chemistry
- Synthetic biology
- Biomimetic chemistry
Background:
- Coacervates, formed by liquid-liquid phase separation (LLPS), serve as model protocells with unique microenvironments.
- Designing simple peptides for self-coacervation is challenging due to complex macromolecular requirements.
Purpose of the Study:
- To design a minimalistic peptide capable of self-coacervation.
- To create a peptide-based microreactor for hydrophobic reactants.
- To develop a supramolecular catalyst mimicking enzymatic activity.
Main Methods:
- Synthesis of a simple dipeptide composed of hydrophobic and histidine residues.
- Induction of self-coacervation and liquid droplet formation.
- Characterization of fibrillar assembly and catalytic activity.
Main Results:
- The designed dipeptide self-coacervates into micrometre-sized droplets.
- These droplets function as microreactors for hydrophobic reactants.
- The peptide also forms catalytic fibrils that mimic esterase activity.
Conclusions:
- A minimalistic peptide design enables self-coacervation and protocell-like behavior.
- The peptide-based coacervates and fibrils offer a strategy for supramolecular catalysis.
- This work has potential applications in enzymology and synthetic biology.
