Q&A with PhD Candidate Farshad Azimi

Tuesday, October 30, 2012
Farshad Azimi
Farshad Azimi, LMP PhD Candidate - Photo Courtesy of Paul Hamel

Why did you choose LMP? I chose the LMP Pathobiology Specialist Program during my undergraduate degree and then decided to pursue my graduate studies within the same department. When I came to Canada I had been a medical student for one and a half years in Iran. Following my acceptance into the University of Toronto’s Faculty of Arts and Science, I chose a program which would strengthen my understanding of the fundamental cellular and molecular mechanisms underlying disease processes, as opposed to the clinical science courses that I had taken previously. Furthermore, I had planned to engage in basic science research with clinically-oriented objectives; LMP just seemed to be the perfect fit.

What are you currently researching? I am currently a graduate student in the laboratory of Professor Jeffrey Lee. Our lab focuses on structural immunovirology. We use biochemical and structural techniques to interpret atomic-resolution details of the biological interactions between host and viral biomolecules. We then use our structural data to predict the functional significance of these biomolecules during their interaction with other molecules, mediating both the biology and the pathology.

My project is focused on understanding the structural determinants of one of HIV-1’s accessory proteins in mediating the pathogenesis of AIDS. More specifically, I am using X-ray crystallography and other structure-determination techniques to understand the interactions between my protein of interest and other host and viral proteins.

How would this research potentially impact society? AIDS has serious social, economic, and health-related repercussions worldwide and in Canada. Globally, every sixteen seconds one person dies from AIDS. At the national level, 22,300 Canadians have died from AIDS and an estimated 65,000 are living with the disease, as of the end of 2008. Despite extensive research on HIV for the past three decades, the knowledge base to develop fully preventive or treatment strategies has fallen short: HIV rapidly evolves around the disruptive effects of available drugs, mutating into new resistant strains. In my research, structural insights obtained into the specific molecular interactions between the HIV and human host proteins will be used for targeted structure-based drug designs and high throughput screening of small-molecule inhibitors. 

What is the most interesting aspect of your research? The most interesting aspect of my research is the fact that I apply some of the most fundamental concepts and tools of physics and chemistry to gain functional insight into the workings of our cells and their interactions with viruses. And, the second most interesting thing is that I get to sound all cool and smart when I get to talk about my work!

How has your supervisor helped you advance your education? If I have to answer in one phrase I would say: “in numerous and tremendous ways”! When I started in the lab, I had little to no experience in the biochemistry and structural techniques that I am now using for my project.

Prof. Lee, personally trained me in different sub-cloning and DNA manipulation techniques, protein expression and purification, protein biochemistry and structural determination methods such as crystallography. In addition, he encouraged me to participate in workshops, training seminars and conferences in computer programming (for biologists) and low-resolution structure determination techniques such as small angle X-ray scattering. Prof. Lee has also provided an amazingly friendly lab environment, which supports information exchange between him and the students on a frequent basis. Both a biochemist and a structural biologist, Prof. Lee provides very helpful suggestions on how to tackle certain difficulties in my project and how and where to look for answers when none seem to be found. In a nutshell, Prof. Lee has been supportive of both my project and my intellectual development towards becoming a scientist.

How do you strike a lab/life balance? I have to make sure I’m not throwing people off when I say I have done that! For me, a lab versus life balance could be defined completely differently compared to someone else’s. I think I have struck that balance to a certain extent, but it doesn’t mean I am not struggling to either maintain or improve it. I do have a few things outside my lab life, that I take both interest and pride in pursuing.

Firstly, I love my music; more specifically, I like playing it. I love my two violins and I keep one of them in my lab. After 8 p.m., whenever I am alone in the lab purifying protein or waiting on an incubation step, I take my instrument out and start practicing. Believe it or not, you can get from 30 minutes to an hour of practice every day if you do it like that. Music aside, I also do drawing and sketches in my free time and I love cooking. While it can be difficult to balance all of this with my research, I really enjoy working in the lab so I never count hours or keep track of my time. Overall, if you’re in it for the right reasons, your graduate years will be filled with a lot of purely amazing and enjoyable seconds, minutes and hours to remember! Trust me!

What are your future aspirations? I am planning to finish my PhD with Professor Lee, publish a few “good” papers (well that part is every graduate student’s wish) and then pursue my medical education at the University of Toronto. However, I know that I will be continuing with clinically-oriented basic science research on the side. I think I need that extra intellectual inspiration that comes from basic science research.

In the long run, I hope to be able to return to research as a professor and have my own laboratory. If you ask in what area, I am going to say structural cancer immunology!