Apr 20th, 1:00 PM - 4:00 PM


Investigation of the Coenzyme Binding Mechanism of Carbonyl Reductase Using Fluorescence

Faculty Sponsor

Dr. Henry A. Charlier


Carbonyl reductase (CR) is biological enzyme that may play a key role in mediating the cytotoxicity and cardiotoxicity of common anticancer drugs currently being administered. CR’s role in the human body is to reduce carbonyl-containing molecules to their respective alcohol in the presence of the coenzyme NADPH. One such group commonly used in treating cancer is the anthracyclines. Unfortunately, administering anthracyclines to patients is limited due to the cardiotoxic effects of its metabolites once processed by CR. A further understanding of CR could lead to drug development that minimizes the activity of CR thus increasing anthracyclinedependent cytotoxicity and limiting cardiotoxicity. Understanding the kinetic mechanism of CR is essential in this process. While previous research has focused on the kinetic mechanism as a whole, little work has been done to measure enzymecoenzyme binding. Being so, determining the quantitative kinetic mechanism of CR binding NADP is of interest and can be done using a technique involving fluorescence. (NIH Grant # P20 RR016454)