Research Projects

Double Helix Swap Mutants

Aug 2025-PRESENT

I will present work for this project at S3 Spring 2025.

AAK1 (1-767) PROTAC Degrader

May-July 2025

In ovarian cancer, the kinase AAK1 promotes tumor survival and resistance to paclitaxel, a standard chemotherapy drug. Paclitaxel treatment increases AAK1 activity and produces a truncated form, AAK1 (1-767), which supports cancer cell survival through kinase-independent mechanisms. This project develops PROTACs to selectively degrade AAK1 (1-767) via the ubiquitin-proteasome system, involving synthesis, purification, and validation of compounds followed by biological testing. The ultimate goal is to enhance chemotherapy effectiveness and overcome drug resistance through targeted protein degradation strategies.

I presented work for this project at UF STRONGER Showcase, UCLA CSU Symposium, URS, and ABRCMS Conference

Wild-Type IDH2

Jan-May 2025

Research aims at understanding the catalytic and structural effects of isocitrate dehydrogenase 2 IDH2 mutations in the progression of cancers of the brain (gliomas) and blood (acute myeloid leukemia). In this work I introduced targeted mutations at specific amino acid residues using site-directed mutagenesis, heterologously expressed and purified human proteins in E. coli and used steady-state kinetics methods to assess the catalytic activity of these mutated enzymes.

I presented work for this project at S3 Fall 2025

Mutated IDH2

Aug-Dec 2024
Isocitrate dehydrogenase (IDH) normally converts isocitrate to alpha-ketoglutarate, but mutations in IDH1 and IDH2 cause the enzyme to produce the oncometabolite D-2-hydroxyglutarate (D2HG), disrupting redox balance and promoting tumorigenesis. These mutations are common in several cancers, including gliomas, leukemias, chondrosarcomas, and cholangiocarcinomas. This study focuses on the IDH2 R172K mutation, a frequent cancer-associated variant that produces high levels of D2HG in certain lymphomas. Using site-directed mutagenesis and kinetic assays, we aim to characterize how this mutation alters IDH2’s structure and catalytic activity, deepening our understanding of its role in cancer development.