Unravelling the Role Amyloid Aggregation Plays in Neurological Disorders
In biology, a molecule’s structure has an incredible influence on its function, determining how and when it can interact with other cellular components. In the past, scientists believed that proteins—the basic building blocks of cells—only existed naturally in two states: unfolded (inactive) or folded (active) conformations.
But we now know there is a third protein structure—one almost exclusively associated with neurological disorders such as Alzheimer’s and Parkinson’s diseases. In people who have these diseases, toxic clumps form when proteins come together in a fiber-like tangle called an amyloid aggregate.
Recently, scientists have begun to speculate that amyloid aggregates may also exist naturally, since many human cells seem able to form and disassemble these fibre-like structures. As Canada Research Chair in Functional RNA and Cellular Stress, Dr. Timothy Audas is trying to shed light on how cells regulate natural amyloid aggregation to better understand the pathology of these debilitating neurodegenerative disorders.
Audas has already discovered that harsh environmental conditions can induce natural amyloid aggregates to form. But unlike their disease-associated counterparts, natural amyloid formation is non-toxic, and actually increases cells’ ability to survive during periods of stress.
Now, Audas and his research team are studying the pathways cells use to adapt to their environmental surroundings using three approaches: they are identifying and characterizing molecules that regulate natural amyloid formation; uncovering stimuli-specific targets of amyloid aggregation; and examining the biological consequences of natural amyloid formation. Their work may lead to new avenues to combat age-related neurological disorders.