Transglutaminases catalyze the cross-linking of proteins, by binding an amine (a lysine bound to a protein or peptide) to the terminal amide of a glutamine bound to a protein or peptide. Transglutaminases are increasingly used in protein labeling systems, where various amino compounds are bound to proteins, giving the modified proteins new properties.

Cytochromes P450 oxidize hydrophobic compounds to increase an organism's ability to eliminate these compounds. The oxidation reactions they catalyze have great potential for biocatalytic applications. To this end, we are experimentally adapting the Bacillus megaterium cytochrome P450 to catalyze industrially relevant reactions.

Dihydrofolate reductases (Dfr) are essential for cell proliferation. Therefore, they are the target of the antibiotic trimethoprim. The emergence of an alternative Dfr, Dfr type B (DfrB), confers insurmountable resistance to trimethoprim. We investigate the evolution and function of this enzyme by combining bioinformatics and experimental methods to inform our design of DfrB-specific inhibitors.

In collaboration with the research laboratories of Jean-François Masson (U. of Montreal) and Denis Boudreau (U. Laval), with the help of organizations such as Instruments Scientifiques Affinité, Héma-Québec and many other collaborators, we are currently developing a combined ELISA and SPR (Surface Plasmon Resonance) approach to quantify and characterize antibodies against SARS-CoV-2.