Grant: Project Grant

In many neurodegenerative diseases such as Alzheimer's, the tau protein comes together to forms large clumps in our neurons called aggregates. These aggregates physically clog up the space in our neurons and interfere with its ability to function normally. We know that these tau aggregates can have different shapes and can form faster or slower depending on the disease. In our work, we are trying to figure out what features of a tau aggregate makes it more or less dangerous to cells. Is it the shape, or how fast it forms or some other property that can really tell us how dangerous a tau aggregate will be? For our studies, we make thousands of different small changes to the tau protein and then determine how this effects the way it aggregates. We use multiple different experiments, performed in test tubes and cell cultures, to examine all the different features of these aggregates and compare them to one another. Our goal is to find out how to make the most and least dangerous tau aggregates so that we can better study how to assist our cells in fighting the tau aggregation occurring in disease with drugs or other treatments.