个人简介

Dr. David Sanders is a member of the Department of Chemistry, and an associate member of the Department of Biochemistry. He joined the faculty in 2001. Dr. Sanders obtained his B.Sc. from the University of Guelph (Co-Op Honours Biochemistry). He received his PhD from the University of Arizona in the lab of Dr. W. Montfort. He then spent 3 years as a PDF in St. Andrews, Scotland, with Dr. J. Naismith. Research in my lab is focused on understanding how proteins function, by studying their atomic resolution structures. Using protein X-ray crystallography as a tool for elucidating structures, we combine structural studies with enzymology, site-directed mutagenesis and computer-aided design of inhibitors to understand how proteins function. The determination of the 3-D structures of proteins and their complexes enable us to answer important questions about how these proteins function, and how they interact with their substrates and each other. At the University of Saskatchewan, we are ideally placed to carry out this research, due to the presence of the Canadian Light Source, Canada's own synchrotron light source, and the Saskatchewan Structural Sciences Center, a facility equipped with instruments for biophysical characterizations of macromolecules. The major area of research in my lab is to understand enzymes that have important roles in pathogenic microorganisms. We are studying these enzymes to determine their function and design inhibitors that could potentially act as lead compounds for drug development. We are studying novel enzymes found in bacteria and other pathogenic microorganisms. The development of multi-drug resistant (MDR) bacteria mean that the current lines of antibiotic agents will become less and less effective against common bacterial infections. It will be important to investigate potential new targets to develop novel ways of combatting pathogenic microorganisms. The bacterial cell wall has long been a target for antibacterial compounds, including the β-lactams. The cell wall of most bacterial species consists of combinations of sugar residues, many of them unique to bacteria. Targeting the biosynthetic pathways that produce the novel sugar residues is an attractive drug target as these pathways will not exist in the host organism, limiting the side-effects. Some of these sugars also exist in other pathogenic microorganisms, increasing their potential as drug targets. Different bacteria also are found that produce their own antibiotic agents. These antibiotics are often very different than other compounds and offer a unique opportunity to study enzyme reactions. These pathways often include unique enzymes involved in their biosynthesis and we are currently studying two biosynthetic pathways. We also study several enzyme systems to fundamental structure-function questions. While these systems may not have any direct applications in human health, the fundamental underlying principles will be important to many systems.