Chaperones as a Novel Target Against Amyloids in Parkinson's Disease

Protein misfolding and amyloid formation is an underlying pathological hallmark in a number of prevalent diseases of protein aggregation, including Parkinson¿s disease (PD), Alzheimer¿s disease and Type 2 diabetes. Most importantly, the severity of these diseases appears to correlate with the degree of the deposition of amyloid aggregates. The misfolding of ¿-synuclein, a protein involved in PD, followed by its aggregation has been shown to be highly cytotoxic and to play a key role in the death of neurons. Thus, the modulation of the aggregation process, promoting the proper folding of ¿-synuclein, may be considered as an attractive avenue for a therapeutic intervention. Indeed, molecular chaperones have been shown to assist in the maintenance of a functional proteome in vivo and to prevent protein misfolding, aggregation and amyloid formation.