Aptamers designed to target α-synuclein, a protein implicated in the pathogenesis of Parkinson's disease due to its propensity to aggregate, were investigated to probe their affinity for the protein as well as their ability to hinder the aggregation of the protein in vitro. Aggregation assays have proven that the presence of the aptamer candidates targeting monomeric α-synuclein stunt the formation of protein fibrils. One promising aptamer from the research, a-syn-1, was successfully packaged into a liposome vesicle modified to cross the blood-brain barrier and used in in vivo applications. Analysis of the liposomes used for the packaging and delivery of the aptamer has provided insight into the loading efficiency and production efficiency of liposome batches.