Student Profile: Augene Park

Research Summary
Biomolecular condensates are membraneless organelles that have been found in cells to regulate cellular biochemical reactions, sequester cellular components, and enhance enzyme kinetics. Intrinsically disordered proteins (IDPs) can form biomolecular condensates under certain conditions, where they phase separate into protein-rich liquid droplets in equilibrium with a protein-poor phase. Currently, my research is focused on biomolecular capture into IDP droplets formed by the disordered N-terminal RGG domain from C. elegans LAF-1. By coupling our RGG constructs with either SYNZIPs to create synthetic coiled-coil interactions or by using the SpyCatcher/SpyTag system for irreversible protein conjugation, we can create protein-protein interactions that allow for client proteins to be recruited into these IDP droplets. I have been investigating the effects that recruited molecules such as GFP and antimicrobial peptides have on IDP droplet properties. In addition, I am exploring how protein structural variations such as recruitment domain placement or linker lengths between domains can affect capture efficiency and phase separation properties of the scaffold-client complex. In the future, I plan to expand my experiments to test other phase-separating proteins, capture/release domains, and different recruited proteins such as enzymes. By doing so, I aim to leverage biomolecular condensates to develop new methods of protein purification, to create novel protein-based drug carriers, and to increase enzyme activity for pharmaceutical biosynthesis.