Alpha-Synuclein misfolding and aggregation are linked to the Parkinson's disease pathology. In the unbound form, α-synuclein is a typical intrinsically disordered protein. It can adopt different conformations depending on the environmental modulators. Many environmental factors promote α-synuclein misfolding and aggregation. Structural variability of aggregated forms correlates with their effects in vivo.

Aggregation of alpha-synuclein (αS) into oligomers is critically involved in the pathogenesis of Parkinson’s disease (PD). Using confocal single-molecule fluorescence spectroscopy, we have studied the effects of 14 naturally-occurring polyphenolic compounds and black tea extract on αS oligomer formation.

The E46K is a point mutation in alpha-synuclein (alpha-syn) that causes familial Parkinsonism with Lewy body dementia. We have now generated a cell model of Parkinsonism/Parkinson's disease (PD) and demonstrated cell toxicity after expression of E46K in the differentiated PC12 cells.