Neurodegenerative disorders caused by prions include Creutzfeldt-Jakob disease and similar disorders in animals such as bovine spongiform encephalopathy in cows, chronic wasting disease in deer, and scrapie in sheep (Imran and Mahmood, 2011; Windl and Dawson, 2012). Prion protein (PrPC) is a normal cellular protein that when mutated becomes misfolded (PrPSc). PrPSc can then convert normally folded PrPC to the misfolded form. Accumulation of PrPSc causes loss of neurons, astrogliosis, and spongiform degeneration resulting in dementia, ataxia, and death. One approach to therapeutic development has been to block or interfere with the conversion of PrPC to PrPSc. TUDCA and UDCA were found to substantially reduce this conversion in cell-free aggregation assays as well as in both chronically and acutely infected mouse ScN2a neuroblastoma cells (Cortez et al., 2015). TUDCA and UDCA also reduced neuronal loss in a prion organotypic slice culture model of intracerebral infection that assesses prion replication occurring ex vivo through infection of brain slices with prion infected brain homogenate. UDCA treatment also reduced astrocytosis and prolonged survival in prion infected male C57BL/6 mice, although whether bile acids interacted with the PrPC to PrPSc conversion or mediated protective effects through some other mechanism is not known.