Skip to Content

Identification of Potential Therapeutics for Parkinson's Disease

Our lab has successfully identified the aggregation-prone amino acid sequence that is important for the aggregation of ɑ-Synuclein protein (ɑS), which is the process responsible for production of Parkinson’s Disease (PD) phenotypes, with symptoms such as impaired motor functions. My goal is to further confirm the role of these sequences in aggregation and identify individual amino acid(s) within that sequence that are important for ɑS aggregation. This will be accomplished using design of ɑS variants with point mutations, created by substituting alanine for amino acids within the aggregation-prone sequence. Thioflavin T (ThT) fluorescence assays, transmission electron microscopy (TEM), cellular assays, and confocal microscopy will then be performed on the purified ɑS variants. This study will further develop understanding of the role of individual amino acid(s) in facilitating ɑS aggregation. In addition, this will advance identification of potential therapeutic targets for the treatment of PD. With this amino acid sequence identified, synthetic molecules can be synthesized to bind and potentially inhibit aggregation of ɑS.