Dr. Masoud Jelokhani-Niaraki

I have pursued my scientific career in several academic institutes and countries. As an undergraduate student my main interest was in organic and biological chemistry, and I had a unique opportunity in working as a research assistant for a few years in the organic synthesis laboratory with Dr. Grikor Terpoghossian in Tehran. During these years, I developed a strong interest in biochemistry and pursued this field in Japan at Saga University as a graduate student in Dr. Michio Kondo’s laboratory. I graduated in 1995 and worked as a lecturer in biochemistry for 1.5 years in Saga University. My research in Japan was focused on peptide ion channels and their conformation and electrophysiological properties in biological membranes. In 1996, I joined the laboratory of Dr. Robert Hodges at the University of Alberta as a postdoctoral fellow and was involved in studies on structure-activity relationships of antimicrobial peptides. I spent a year at Brandon University as an assistant professor and then joined the Department of Chemistry at Wilfrid Laurier University in 2001 as an assistant professor of Organic and Biochemistry. At present, my research activity is concentrated on two main areas. In one research program, we are studying the conformation and biophysical properties of the mitochondrial uncoupling proteins to elucidate the role of transmembrane segments in ion transport and protein folding. In the second program, we are investigating the mechanism of interaction of natural and synthetic cyclic cationic antimicrobial peptides with biological membranes as a crucial step in their biological activity. In both programs we are utilizing chemical protein synthesis and biophysical techniques. Peptide molecules are synthesized by employing solution and solid phase techniques, and purified and analyzed by HPLC and mass spectrometry. A combination of biophysical techniques such as fluorescence and circular dichroism spectroscopy, isothermal titration calorimetry, patch clamp, and tensiomety, are used for these studies.

Departmental website

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