Dr. Michael Woodside received a Fellowship from the John Simon Guggenheim Memorial Foundation at a reception in New York City in May.

When asked about how it feels to be one of three Canadians to receive a fellowship this year, Dr. Woodside stated "it is an honour but humbling when you look at the people who have won before."

And it is an honour. Dr. Woodside is the first University of Alberta fellow since the 1970s and the first Alberta recipient in the natural sciences.

The Guggenheim Fellowship will provide him the opportunity to travel during his sabbatical to labs in Boulder, CO; Bethesda, MD; Berkeley, CA; and Eugene, OR where he will learn new techniques in bioinformatics, classical biochemistry and theoretical physical chemistry to apply to his current research. The lab in Eugene is one of his collaborators on a current project funded by Alberta Innovates via the Alberta Prion Research Institute.

The focus of his Guggenheim Fellowship project will be on the folding and misfolding of proteins at the microscopic level and how evolution has shaped and changed the process. Two of the labs he will be visiting have traced proteins back billions of years to when only bacteria existed.

The Guggenheim Fellowship is just one of his many research successes of late. Dr. Woodside's research has recently been published in Nature Communications, Nature PhysicsProceedings of the National Academy of Sciences and Science, four of the most prestigious scientific journals in the world. Publishing in high-impact journals helps to promote his work, the University of Alberta and the importance of basic research.

In particular, his publication in Science laid the groundwork for the Guggenheim Fellowship. Dr. Woodside developed a method to use so-called laser tweezers to pull apart prion proteins to look at them at a molecular level. He is the only researcher in Alberta and one of very few in the world using laser tweezers to study prion proteins, aiming to understand how they change from their normal to the infectious state where they can cause disease.

The ability to pull apart prion proteins gives Dr. Woodside the advantage of being able to see the details of how the protein's structure changes. This is important because researchers do not know why or when the molecules transition to become misfolded and infectious. Scientists aren't even certain of the normal function of the prion protein. All humans have prion proteins, so there must be a reason we have them.

Human prion diseases are often referred to as a one-in-a-million disease. Trying to find the rare event of protein misfolding amongst trillions of molecules is a very difficult task. Dr. Woodside's usage of the laser tweezers allowed him to stick two protein molecules together to generate a misfolded protein to measure the amount of time it takes to misfold and to look at the properties of the transition from normal to misfolded state.

Dr. Woodside's lab is the first in the world to see and measure the transition in a prion protein from a normal state to a misfolded state.

Previous studies of transition paths could only use computational models. The research done in Dr. Woodside's lab was the first experiment that successfully measured the transition path in a molecule. Using the laser tweezers allowed Dr. Woodside's lab to see what's happening in the molecule, not just a model, revealing that the misfolding happens much more slowly than initially thought.

The significance of this is that his lab can now see thousands of transitions in the molecules. The transition from normal state to misfolded state is no longer predicted by theory. By looking at the transitions and seeing where things go wrong, this could lead to identifying new targets and antibodies or treatments for prion diseases.

It is this search at the molecular and microscopic levels that could lead to breakthroughs in prion and protein misfolding diseases. By looking at proteins from an evolutionary standpoint, it will help to see how features in proteins in existing species developed in the past.

His longer-term goal is to develop a single molecule assay to detect when and how a molecule propagates to another molecule. This is significant in two ways: to mechanistically see how the proteins misfold and direct screening for potential drugs through the propagation of misfolded proteins.

As Dr. Woodside puts it: 'you never know what is going to be the foundation of the next big technology. No one has been able to solve prions with traditional methods. Using this unique technique might one day lead to being able to treat prion and prion-like diseases.'

Alberta Innovates is proud to fund the innovative research of Michael Woodside and other prion researchers in Alberta.