Utilising Fluorescence Microscopy to Visualise the Dynamics and Interactions of Molecular Chaperones and α-Synuclein

In Parkinson's Disease (PD), the protein α-synuclein and its early stage oligomers have been implicated as the primary cause of neuronal toxicity. Molecular chaperones play an important role in maintaining protein homeostasis in such diseases. The dynamic nature of the chaperone cycle and its interaction with the α-synuclein substrate makes it difficult to characterise by traditional biochemical techniques. Using a range of fluorescence microscopy approaches we show that α-synuclein exists in a concentration dependant dynamic equilibrium between monomeric and oligomeric states, with rapid exchange of subunits between species.