Our research is focused on elucidating the structure function relationship of cytochrome P450 enzymes in lung cancer using biochemistry, cell biology, and X-ray protein crystallography.
Members of the cytochrome P450 CYP4F family belong to a group of w-hydroxylases which produce important lipid mediators in the human body. One of these lipid mediators is the molecule 20-hydroxyeicosatetraenoic acid (20-HETE) which is regulating the blood pressure and promotes the formation of new blood vessels in healthy humans. In cancer, 20-HETE promotes cell proliferation and invasion and thus, 20-HETE generating cytochrome P450 enzymes might be exciting new drug targets for cancer treatment.
We use a combination of cell biology and biochemistry to assess the role and function of CYP4F enzymes in oncogenesis and cancer progression. Moreover, we use X-ray protein crystallography to solve structures of CYP4F enzymes for directed design of selective drugs which only inhibit the target and not any of the other 56 P450s in the human body.
- Diploma in Molecular and Human Biology from Saarland University (Germany), 2012
- PhD in Biochemistry from Saarland University in the laboratory of Rita Bernhardt (Germany), 2012-2016
- Postdoctoral training at Saarland University (Germany) in the laboratory of Rita Bernhardt, 2016-2017
- Postdoctoral training at the University of Michigan in the laboratory of Emily Scott, 2017-2021
School of Pharmacy Department of Pharmaceutical Sciences
Center for Pharmacogenetics
Salk Pavilion 3rd floor, room 305
335 Sutherland Dr
Pittsburgh, PA, 15261