The Impact of Spermine on Alpha-Synuclein Aggregation and Cell Viability in Parkinson's Disease
Alpha-synuclein (αS) is a dopamine-regulating protein in the brain that can form aggregates, clusters of misfolded proteins, and cause neurodegeneration in the form of Parkinson’s Disease (PD). This research project explored the hypothesis that αS aggregates in the presence of the polyamine spermine—of which there are elevated levels in PD patients—induces toxic forms of αS aggregates and promotes cell death. With a better understanding of the interactions between naturally existing brain chemicals and the protein that causes PD, we will be that much closer to finding more effective treatments, or possibly a cure.
I went about researching αS with three assays: an MTT cell viability assay, a ProteoStat aggregation assay, and immunofluorescence staining. We found that spermine can be shown to increase the level of aggregation of αS, as well as decrease cell viability, implying increased toxicity. These findings provide a new point of attack for Parkinson’s Disease research. With spermine now available as a clear target, we can work on developing other biomolecules that will inhibit the effects that spermine has on protein aggregation. These findings open the door barring a cure incrementally more, and give us a stepping stone from which to launch new hypotheses and research projects.