Originally posted on the Canadian Blood Services Research, Education, and Discovery (R.E.D.) blog by Dr. Geraldine Walsh and republished with permission and minor edits. Read the original article on the R.E.D. blog.
Congratulations to Alexandra Witt on writing the winning entry of this year’s Lay Science Writing Competition, “Science behind the scenes!” Witt identified high school students as her target audience and wrote an engaging piece that sheds light on the questions scientists ask when developing a new drug.
When you think of proteins, you probably think about chicken, steak, or that new tofu dish your friend made. If I’m lucky, you think about those tiny molecules that your teacher mentioned in biology class. My work is all about those tiny molecules.
In my lab at the Centre for Blood Research, I spend my days (and nights) making proteins and testing them to see if they have what it takes to bust up a blood clot and save a life. It’s a long road to get from a test tube to a treatment, and it involves a lot of questions.
The first question is: What do we want our drug to do?
Heart attacks and strokes are the leading causes of death worldwide and usually involve a clot, which blocks the flow of blood. If we want to bust those harmful clots, we might want to use a drug that initiates or accelerates the normal clot-busting process. For that, it’s best to mimic a protein that is already in our blood. In my case, I went with a protein called clotting factor X, which is normally part of the clot formation cascade, but has a surprising and contradictory second function as an accelerator of the clot-busting process.
The second question is: How do we capitalize on that clot-busting function?
A protein like factor X has two roles in the body; first, it’s involved in the formation of a blood clot, and second, it’s involved in clot busting. Different signals tell factor X what role it needs to be in, or what hat it needs to wear, depending on the body’s needs. If we only want factor X to wear the clot busting hat, we need to start at the very beginning and edit the protein’s DNA. We need to make changes to the protein’s blueprint that say “you only get one hat”. Once we have our new blueprint, it’s time to give it to the construction workers.
The third question is: How do you build a protein?
In our lab, we have colonies of cells, minus the hard hats and reflective vests. Just like they do in our body, cells in a petri dish or fancy flask can grow and divide and make proteins. We can collect those proteins, purify them, and even run experiments to prove that they’re the proteins that we want. Then, we can test them.
The fourth question is: How do we know if our drug is any good?
In my lab, I test mutated factor X in test tubes and in mice. I have to make sure that it can’t remove its clot-busting hat and accidentally make a clot, and I have to make sure that it can speed up the clot-busting process.
If my drug works, I could fill a major gap in patient care and save thousands of lives each year. It’s a pretty fulfilling job.
My question to you is: When will you start your scientific journey?
About the author:
Alexandra Witt is a first year Masters student under the supervision of Dr. Ed Pryzdial at the University of British Columbia’s Centre for Blood Research. Her project revolves around the creation of a new drug to bust up the blood clots that cause heart attacks and strokes. Alexandra joined the Canadian Blood Services lay writing competition as a means to creatively explain her graduate work to her friends, family, and the greater Canadian Blood Services’ community.
Read more about the Lay Science Writing Competition and stay tuned for the other entries, to be published soon:
Science behind the scenes: Lay Science Writing Competition winners announced
Lay Science Writing Competition runner up (2nd place): The greatest tool in research
The 2021-2022 Canadian Blood Services Lay Science Writing Competition was organized by the Canadian Blood Services’ Centre for Innovation with welcome support from the Centre for Blood Research at the University of British Columbia and Science Borealis.