Biochemistry / Psychology / Math
Project title: Mechanism of neurotoxic α-synuclein oxidation by dopamine in Parkinson’s disease
Mentor: Kathryn Matera
The first half of this spring was spent trying to repeat my results from winter term. In January I had developed a thioflavin T assay protocol for measuring the amount of protein aggregation in samples. I then used this test to measure to what degree dopamine derivatives I had observed over the summer, namely norepinephrine, were able to break apart alpha synuclein aggregations. As talked about in my proposal, breaking apart these aggregates may be a key step in the progression of Parkinson’s disease because they create smaller soluble aggregates called oligomers that can be toxic to cells. My winter term results showed that norepinephrine was in fact a disaggregating agent, even better than dopamine itself. This semester I thought it would be easy to replicate this, but I was wrong. Ultimately I had to run many trials and alter the protocol in several ways to get it to work again. Dr. Matera had told me several times that experiments always work the first time, but never the second. It was quite a growing experience to have this actually happen to me as I worked on my project. The second half of the semester was spent developing an SDS-PAGE and silver staining technique that could be used to identify the types of oligomers that are generated after large insoluble inclusions are broken apart. I preformed this using insulin as a model since it is much less expensive than alpha synuclein and hope to use the protocol to generate some data in the fall. All of these pieces are coming together into what will ultimately be a theory about how disaggregation occurs and how oligomers form with these species.
Dr. Ann J. Cahill
Professor of Philosophy
Spence Pavilion 111
2340 Campus Box
Elon, NC 27244
Phone: (336) 278-5703
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