# POMPOMS: Crosslinked Biomolecular Condensates as a Versatile Platform for Multifunctional Protein Microparticles

## TL;DR

Researchers developed a new method to create microparticles from proteins using droplet crosslinking, enabling versatile and functional materials.

## Contribution

A novel method for creating multifunctional protein microparticles using crosslinked biomolecular condensates.

## Key findings

- Microparticle size was controllably varied from <1 to >40 μm using condensate coalescence.
- Cargo proteins were successfully captured using the SpyCatcher/SpyTag system.
- A thermostable alcohol dehydrogenase was immobilized with 31% retained enzymatic activity.

## Abstract

Protein-based microparticles
are promising materials for applications
such as biocatalysis and biomolecular capture, yet their fabrication
by existing techniques remains challenging due to protein denaturation
or lack of spatial control. Here, we present a method for synthesizing
microscale protein-based materials by chemically crosslinking biomolecular
condensates. Leveraging the liquid–liquid phase separation
behavior of intrinsically disordered RGG domains, we sequestered RGG-tagged
fusion proteins into droplets, then we solidified them into porous
microparticles using the homobifunctional, amine-reactive crosslinker
BS3. By modulating protein concentration and condensate
coalescence, we controlled microparticle size from <1 to >40
μm.
We then demonstrated three encodable functionalities: We used the
SpyCatcher/SpyTag system to capture cargo proteins, we crosslinked
core–shell condensates to generate microparticles with controlled
spatial organization, and we immobilized a thermostable alcohol dehydrogenase
with 31% retained enzymatic activity. These POMPOMS (protein-based,
self-organized microparticles of multifunctional significance) represent
a sustainable, tunable platform for versatile protein-based materials.