With applications in biomedicine, biomaterials and advanced biomanufacturing
What if the answer to improving the quality of life and combating neurodegenerative diseases could also help answer one of humanity’s oldest questions: what is the origin of life? The connection lies in the evolutionary field of protein editing in biotechnology.
Dr. Ned Budisa, a professor and (Tier 1) Canada Research Chair in chemical synthetic biology at the University of Manitoba, is taking a closer look at protein editing and is exploring more efficient approaches. According to Budisa, if we can understand the chemical origin of the transformation of one protein with normal physiological functions into one with pathological functions, we can replace that one building block and prevent harm to our health.
The problem is the lack of efficient systems. Currently, the field relies on heat-loving translation enzymes (synthetases) to build engineered proteins. These enzymes are extremely rigid, and evolving them to recognize and load alternative chemical building blocks is a massive hurdle. This makes the entire process expensive, inefficient and hard to scale.
Budisa and his research group, including Dr. Hamidreza Karbalaeiheidari, a visiting professor at the Department of Chemistry, have developed a novel approach to protein editing.
The key is cold-adapted enzymes. The researchers’ new approach explores biology adapted to extreme cold, reducing the cost and making the process more energy-efficient and sustainable.
The vision for the future is scaling the platform to produce increasingly complex designer proteins. This could have applications in biomedicine, biomaterials and advanced biomanufacturing.
To learn more about Budisa and his team's research, please watch the following video on the Faculty of Science's YouTube channel.
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