With predominant focus on the role of the protein α-synuclein, given its increased tendency to form neurotoxic oligomeric and fibril species, this thesis investigates aptamers as a Parkinson's Disease (PD) therapeutic generated specifically for the detection and inhibition of monomeric α-synuclein. Aptamers are single stranded oligonucleotide sequences designed for the recognition of target structures with high affinity and selectivity. Binding affinity and conformation analysis of five aptamer sequences, ASYN(1-5), for monomeric α-synuclein were evaluated through various detection methods. ASYN2, having the highest affinity for monomeric α-synuclein, discriminated against similarly structured proteins, preferentially binding with monomeric α-synuclein. ASYN2 truncations, exploiting potential binding domains within the aptamer, yielded six minimer sequences labelled A2m(1-6). Fibril inhibition assays determined both ASYN2 and A2m3 displayed inhibition potential at 1:1 molar ratios of aptamer to protein. Further investigation into ASYN2 and A2m3 could reveal its application as a PD therapeutic.