ISSUE #1 : 2019-2020
How do you break down a protein? I was pleased to have remembered from my undergraduate days that enzymes are the catalysts in molecular reactions and key to breaking down larger macromolecules. Using enzymes as the ‘scissors’, medical researchers can cut apart proteins; however, enzymes will also cut themselves up in the process, creating samples that have both the proteins of interest and a lot of enzyme pieces. Essentially, these samples are ‘tainted’ from the extra enzyme pieces that are created when the enzyme cuts itself. The team uses a process called ‘enzyme immobilization’ to keep the enzymes from splitting themselves while they are splitting up a larger protein molecule (essentially keeping the scissors from cutting themselves up). Although this technique is widely used in proteomics, Ghafourifar’s lab is creating an improved version called ‘capillary electrophoresis’, where immobilized enzymes are strategically placed inside of a glass capillary tube. Subject proteins are then passed through the immobilized-enzyme capillary tube, and the resultant fragments are nearly completely free of contamination. In this way, Golfam’s team is optimizing the immobilized-enzymatic function of proteomics, and developing a critically important tool for use in diagnosing and identifying protein-based diseases. Ghafourifar’s undergraduate student Kaeden Teindl, whose work is part of the Immobilized Enzyme Reactor (IMER) project, won both the 2019 UFV undergraduate research award, and first place at the Canadian Chemical Society’s 2019 meeting for his poster presentation. Says Golfam, “Kaeden is working with me on the academic publication of this work, he will be graduating at the end of this fall“. As Teindl moves on to graduate studies, Golfam looks forward to cultivating an interest in proteomic research in a new cohort of chemistry undergraduates. As a leader in this technical field, her prospective students have much to gain from the opportunities that she has to offer.
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