The development of neurodegenerative diseases is an ever increasing risk faced by modern society as aging populations rise globally. For complex diseases such as Alzheimer's Disease (AD) or Parkinson's Disease (PD) the prospect of finding a cure within the immediate future is unlikely. These complexities arise primarily from the interactions of the protein of interest each of the diseases, which in the case of typical and atypical PD is α-synuclein (α-syn). Thought to be involved in neuronal vesicle recycling in its monomeric α-helical state, change to a β-sheet conformation allows α-syn to misfold, creating oligomers and eventually aggregates which form the initial bedrock for inclusion bodies. One of the more fascinating features of pathological α-syn is the difference in inclusion body composition and cell type affected in typical and atypical PD variants. For instance within Multiple System Atrophy (MSA), an atypical PD variant, α-syn aggregates form Glial Cytoplasmic Inclusions (GCIs) the composition of which differs from the Lewy Bodies (LB) formed in PD, and are largely found in oligodendrocytes. Unlike neurons, oligodendrocytes normally express only minimal amounts of α-syn which does not alter even after GCIs are formed, indicating acquisition of α-syn from an external source. How oligodendrocytes acquire pathological α-syn and the mechanisms by which the protein is able to spread within the central nervous system (CNS) are topics currently with more questions than answers. Thus the primary focus of the thesis is to investigate potential models of α-syn spread in order to develop future novel targets to slow disease progression. [...]