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The Ernesto Freire Lab studies the use of novel drugs to treat disease. Our research has resulted in the development of a thermodynamic platform for drug discovery and optimization. Our aim is to achieve high binding affinity and selectivity as well as appropriate pharmacokinetics with the platform. We are currently focusing on drug targets such as HIV/-1 protease inhibitors (HIV/AIDS), plasmepsin inhibitors (malaria), HCV protease inhibitors (hepatitis C), coronavirus 3CL-pro protease inhibitors (SARS and other viral infections), HIV-1 gp120 inhibitors (HIV/AIDS), chymase inhibitors (cardiovascular disease) and beta lactamase inhibitors (antibiotic resistance).
The Structural Enzymology and Thermodynamics Group uses a combination of molecular biology, biochemistry and structural biology to understand the catalytic mechanisms of several enzyme families. Additionally, researchers in the group are studying protein-ligand interactions using structural dynamics. They are able to apply their knowledge of the mechanisms of these enzymes and of binding energetics to develop targets for drug design.
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