Student Major/Year in School
Biology, third year
Faculty Mentor Information
Ho Leung Ng, Department of Biochemistry, Kansas State University
Abstract
Aromatase (CYP19) is an enzyme that converts androgens into estrogens. It is a drug target to treat hormone-dependent breast cancer, yet current therapeutics often result in patient health deterioration due to unwanted side effects. We want to recombinantly express high yields of stable aromatase to co-crystallize with our new, potent inhibitors. These crystals will be used to produce a 3-D structure to visualize the protein-inhibitor complex. We hope that the structure will help us understand the interactions that are essential for drug potency. We currently produce 1 mg/mL of protein. We hope to increase the stability with mutants A419S, G156A, L240S, and V80S. Stable aromatase increases the likelihood of producing protein crystals. With the 3-D structure obtained from the protein crystals, we can design novel inhibitors as potential candidates to treat hormone-dependent breast cancer.
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License
Recommended Citation
Avila, Bryant (2019). "Production and Purification of Aromatase for Co-Crystallization," Kansas State University Undergraduate Research Conference. https://newprairiepress.org/ksuugradresearch/2019/posters/1
Production and Purification of Aromatase for Co-Crystallization
Aromatase (CYP19) is an enzyme that converts androgens into estrogens. It is a drug target to treat hormone-dependent breast cancer, yet current therapeutics often result in patient health deterioration due to unwanted side effects. We want to recombinantly express high yields of stable aromatase to co-crystallize with our new, potent inhibitors. These crystals will be used to produce a 3-D structure to visualize the protein-inhibitor complex. We hope that the structure will help us understand the interactions that are essential for drug potency. We currently produce 1 mg/mL of protein. We hope to increase the stability with mutants A419S, G156A, L240S, and V80S. Stable aromatase increases the likelihood of producing protein crystals. With the 3-D structure obtained from the protein crystals, we can design novel inhibitors as potential candidates to treat hormone-dependent breast cancer.
