Alpha-Synuclein aggregation in Parkinson’s Disease.
Rheia Reader
The ability of polypeptides to fold into a functional, three-dimensional structure forms the basis of normal cellular and organ function, however, when this fundamental process goes awry it forms the basis of neurodegenerative diseases. Nearly 1 in 6 people have a neurological condition and these diseases can be debilitating and incurable. Parkinson’s Disease (PD) is the second most common neurodegenerative disease that is known as a movement disorder, but that is also characterized by additional non-motor associated symptoms. The pathophysiological hallmark of PD is the misfolding and aggregation of the protein α-synuclein (α-Syn) and the accompanying loss of neurons that produce dopamine in the brain. There are currently no proven therapies for PD and management options consist of symptom relief. Through the development of multidisciplinary approaches (including nuclear magnetic resonance, high-resolution imaging and animal models of disease), scientists have made great strides in our understanding of the chemical, genetic and molecular basis of PD. Although it is commonly accepted that aggregation of α-Syn is key in the pathogenesis of PD, the extent to which its aggregation plays a causal role in neurodegeneration is still a matter of intense investigation. This review will provide a critical assessment of the importance of α-Syn aggregation in PD and discuss the experimental approaches and current and future therapies for this neurodegenerative disease. Expanding our knowledge of the role of protein aggregation in the pathophysiology of PD is critical for the identification of biomarkers for early disease detection, as well as for the development of novel and specific therapeutic approaches.
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