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How modifications to proteins lead to Parkinson's Disease

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Parkinson’s disease is a neurodegenerative disease characterized by inclusions of a small intrinsically disordered protein (14 kDa), α‐synuclein (AS) in Lewy Bodies. Modifications to AS, such as point mutations (A30P, A53T , E46K), phosphorylation of Tyrosine 125 and Serine 129, N-terminal acetylation as well as C‐terminal truncations might affect functioning of the protein as well as its aggregation behaviour into amyloid fibrils. However, detailed mechanistic understanding of the molecular events that lead to the conversion of soluble protein into insoluble aggregates is currently lacking for AS. I will give a short introduction to neurodegenerative diseases in general and explain how my research aims to elucidate the mechanisms that operate in Parkinson’s Disease.

This talk is part of the Darwin College Science Seminars series.

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