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Wilfrid Laurier University Faculty of Science
October 21, 2017
Canadian Excellence
Dr. Masoud Jelokhani-Niaraki

Dr. Masoud Jelokhani-Niaraki

Professor, Chemistry and Biochemistry

Contact Information
Phone: 519.884.0710 ext.2284   |  lab ext.2345/2346
Fax: 519.746.0677
Office Location: BA303C

Languages Spoken


Academic Background
BSc (Honours), Chemistry, Sharif University of Technology, Tehran, Iran
MSc, Organic and Biological Chemistry, Saga University, Saga, Japan
PhD, Biophysical and Biological Chemistry, Saga University, Saga, Japan
Postdoctoral Fellow, Protein Engineering Network of Centres of Excellence (PENCE), University of Alberta

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 ion transport properties of the mitochondrial uncoupling proteins to elucidate the physiological roles of these proteins. In the second program, we are investigating the mechanism of interaction of natural and synthetic 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.
Additional Information

Courses in 2016-2017

Fall Term 2016:

CH332  Biophysical Chemistry

CH456  Medicinal Chemistry

Winter Term 2017:

CH432  Physical Biochemistry of the Cell

CH459  Biochemistry III: Membrane Transport,...