The abnormal accumulation of the intracellular protein a-synuclein has been implicated in the pathogenesis of several neurodegenerative disorders, including Dementia with Lewy Bodies (DLB), Lewy Body variant Alzheimer's Disease (LBVAD) & Parkinson's Disease (PD). In these diseases, known as synucleinopathies, the accumulation of aggregated a-synuclein in the cytoplasm, known as Lewy inclusions, is correlated with cellular dysfunction and death. Although the presence of Lewy inclusions are used as a marker for a definitive diagnosis of synucleinopathies, their specific role in neurodegeneration still remains unclear. The Unni lab has discovered a previously unrecognized function for the protein a-synuclein in repairing nuclear DNA damage. Based on this discovery, we have proposed a new hypothesis that during disease, a-synuclein protein is sequestered in cytoplasmic Lewy bodies, decreasing its nuclear DNA damage repair function and potentially leading to cell death of Lewy body-containing neurons. We have examined which confirmations of DNA a-synuclein preferentially binds for further insight into a-synuclein's normal function in the nucleus.