B.S. (Louisiana State University, USA, 2002)
Ph.D. (University of Texas, Austin, USA, 2010)
Postdoc (University of Illinois, Urbana-Champaign, USA, 2011-2016)
Office: Otto Maass 222
Phone: (514) 398-3637
Lab: P&P 312
Email: christopher.thibodeaux [at] mcgill.ca
Our research applies a diverse set of experimental tools spanning the realms of biochemistry, analytical chemistry, biophysics, molecular biology, and bioinformatics to study the biosynthesis of antimicrobial natural products and the biological processes that contribute to bacterial virulence and pathogenesis.
Combatting Drug Resistant Human Pathogens
Natural products are chemical compounds made by living organisms that serve numerous biological, ecological, and anthropological functions – most notably as medicines to treat a variety of human illnesses. The majority of all drugs approved for human use are either natural products or are synthetic derivatives of natural products. In recent years, however, many of the natural products that have been traditionally used to treat human bacterial infections have lost their effectiveness due to the widespread emergence of antimicrobial resistance. In light of this daunting threat, novel antimicrobial compounds and strategies are urgently needed.
Our research program tackles these challenges by 1) illuminating the mechanistic principles of enzymes that construct antimicrobial natural products and 2) by investigating the biophysics of proteins that contribute to the virulence of bacterial infections through the formation of biofilms. These two processes are joined by their common reliance on protein-protein interactions, yet many knowledge gaps exist in our understanding of these interactions and how they ultimately contribute to biological function. Our research seeks to bridge these gaps by developing high-resolution biomolecular mass spectrometry approaches to provide unprecedented levels of functional insight into enzyme systems. Specifically, we discover and characterize the structures of novel peptide antibiotics, unravel the biosynthetic pathways of peptide-modifying enzymes, correlate enzyme structural dynamics with biological function, and identify and characterize the role of intermolecular protein-protein interactions and conformational changes in biosynthesis and biofilm formation. This challenging work will provide a critical foundation for the discovery of new peptide antibiotics, the engineering of biosynthetic systems to produce new molecules, and for the development of strategies to inhibit protein-protein interactions that contribute to bacterial infections.