Submission Date

7-23-2026

Document Type

Paper- Restricted to Campus Access

Department

Neuroscience

Faculty Mentor

Erica Gorenberg

Comments

Presented during the 28th Annual Summer Fellows Symposium, July 24, 2026 at Ursinus College.

Project Description

Neurodegenerative diseases are complex disorders, with a spectrum of patients, as well as symptoms that are broad and often varied. A hallmark of many of these diseases is misfolded proteins, which can then aggregate. Proteins act as molecular workers of the body, having specific jobs related to their structure, and sometimes these structures can be disturbed, causing a malformed protein to be produced. The body combats these errors with another kind of protein, a chaperone protein, which can either correct or eliminate misfolded proteins. The protein that I will be focusing on is misfolded in Parkinson's disease, alpha-synuclein; this protein aggregation contributes to loss of motor function, a characteristic of Parkinson's. In the Summer Fellows program, I will assess the interaction between the disease protein alpha-synuclein and the chaperone proteins DNAJB6A and DNAJB1 using a yeast two-hybrid assay.  This method works by splitting a transcription factor, a molecule that controls gene expression into two domains: an activating domain and a binding domain. These domains will attach to the target gene, allowing my ampicillin-resistant plasmid to grow on plates with ampicillin added. I will use the yeast model organism to assess alpha-synuclein protein misfolding using a survival assay.

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