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POMPOMS: Crosslinked biomolecular condensates as a versatile platform for multifunctional protein microparticles
Augene S Park1, Erika A Ding1, Benjamin S Schuster1
1Department of Chemical and Biochemical Engineering, Rutgers, the State University of New Jersey, Piscataway, NJ 08854.
Biorxiv : the Preprint Server for Biology
|July 16, 2025
Summary
Researchers developed a new method to create protein microparticles using phase separation and chemical crosslinking. This technique allows for controlled size and versatile functionalities, offering a tunable platform for various applications.
Area of Science:
- Biomaterials Science
- Protein Engineering
- Chemical Engineering
Background:
- Protein-based microparticles are valuable for biocatalysis and biomolecular capture.
- Current fabrication methods face challenges like protein denaturation and lack of spatial control.
Purpose of the Study:
- To develop a novel method for synthesizing protein-based microparticles with controlled size and functionality.
- To overcome limitations of existing protein microparticle fabrication techniques.
Main Methods:
- Utilized liquid-liquid phase separation of intrinsically disordered RGG domains to form protein droplets.
- Chemically crosslinked these droplets using BS3 to create porous microparticles (POMPOMS).
- Modulated protein concentration and condensate coalescence to control microparticle size.
Main Results:
- Successfully synthesized protein-based, self-organized microparticles of multifunctional significance (POMPOMS).
- Controlled microparticle size ranging from <1 to >40 μm.
- Demonstrated functionalities including cargo protein capture, spatial organization, and enzyme immobilization with retained activity.
Conclusions:
- The developed method provides a sustainable and tunable platform for versatile protein-based materials.
- POMPOMS offer a promising solution for advanced applications in biocatalysis and biomolecular capture.
- This approach enables precise control over microparticle properties and functionalities.
