In Dr. Brian Paegel's laboratory, I am working to advance solid-phase DNA-encoded library high-throughput screening technology. My current aim is to adopt bead-based DEL technology onto a novel magnetic microparticle scaffold. These particles are compatible with a wide range of generalized commercially available bead handling instruments generating a distributable and fully customizable small molecule screening platform. Ultimately, my goal is to transform powerful DEL high-throughput screening technology into an accessible tool for small molecule drug discovery.

In Dr. Paul Weer's research laboratory, I studied the oligomeric nature of apolipoprotein A-I. I designed, expressed, and characterized various C-terminal domain mutant proteins to assess the individual and collective role of charged residues in self-association with other apoA-I monomers. Using structural biological techniques including FPLC, chemical crosslinking, CD spectroscopy I identified select lysine and glutamate residues participating involved in intra- and/or intermolecular electrostatic interactions. These interactions stabilize the disordered C-terminal domain, which is essential for scalable oligomerization and regulation of lipid solubilization activity.