# Sequence‐Modulated Active Tripeptide Condensates for Tandem Catalysis

## TL;DR

Researchers developed tripeptide coacervates that mimic cell organelles, enabling controlled chemical reactions in artificial cells.

## Contribution

The study introduces tunable tripeptide coacervates with enzyme-regulated phase separation for compartmentalized catalysis.

## Key findings

- Tripeptide coacervates exhibit enzyme-regulated phase separation and can sequester both hydrophobic and hydrophilic molecules.
- These coacervates enable tandem catalytic reactions in aqueous conditions within artificial cells.
- The system demonstrates potential as functional microreactors with biomimetic properties.

## Abstract

Biomolecular condensates formed via liquid‐liquid phase separation function as dynamic organelles that are vital to regulating cellular activities. Peptide‐based coacervates have emerged as appealing candidates to resemble key properties of biomolecular condensates. However, their application as adaptive organelles has been hindered by structural complexity and limited control over phase‐separation. Here, we present short tripeptide coacervates with tunable phase‐separation behaviors governed by composition and peptide sequence, significantly reducing molecular complexity. These tripeptide condensates exhibit enzyme‐regulated phase‐separation, closely mimicking the dynamic nature of biomolecular condensates. A key attractive feature of the tripeptide coacervates is their capability to sequester both hydrophobic active species and hydrophilic enzymes. This unique property enables the execution of confined tandem reactions in aqueous conditions. When incorporated into membrane‐bound artificial cells, this tripeptide coacervates serve as adaptive sub‐organelles, orchestrating compartmentalized catalytic cascades. This work highlights the potential of minimalistic peptide systems as functional microreactors with biomimetic and catalytic capabilities.

Sequence‐modulated tripeptide coacervates mimic biomolecular condensates with controllable, enzyme‐regulated phase separation. They co‐sequester hydrophobic active species and hydrophilic enzymes, enabling tandem catalysis in aqueous media. Incorporated into artificial cells, they function as adaptive sub‐organelles, orchestrating compartmentalized reactions, demonstrating minimalist peptide systems as tunable, functional microreactors with biomimetic and catalytic capabilities.