Annulé / Canceled
Chris Thibodeaux, Ph.D.
Department of Chemistry
Investigating Antimicrobial Peptide Natural Product Biosynthesis with Mass spectrometry
Natural products have proven to be a reliable source of biomedically relevant compounds. Understanding the enzymatic mechanisms of natural product biosynthesis is critical for studies aimed at engineering the structures of these molecules and for providing sustainable routes to complex molecule synthesis for biomedical needs. Using hydrogen-deuterium exchange mass spectrometry (HDX-MS), we recently revealed the important role played by protein conformational dynamics during the biosynthesis of antimicrobial lanthipeptides. Overall, the data highlight the broad utility of structural mass spectrometry approaches for revealing the biophysical properties and enzyme structural dynamics that likely play a widespread role in regulating peptide natural product biosynthesis.
Christopher J. Thibodeaux is a native of Louisiana, where he graduated valedictorian from Louisiana State University. He completed his Ph.D. in the lab of Hung-wen Liu at the University of Texas, where his research focused on elucidating the mechanisms of enzyme catalysis. Following postdoctoral work to study single molecule spectroscopy and natural product biosynthesis at the University of Illinois, he began his independent career in the Chemistry Department at McGill University. His research is broadly aimed at discovering novel antimicrobial compounds, understanding the molecular mechanisms of peptide biosynthetic enzymes, and engineering new-to-nature peptides with novel biological activities.
Date(s) - March 17, 2020
6:00 pm - 9:00 pm
Emplacement / Location
Université de Montréal - Pavillon Jean Coutu (S1-151)