Small molecules attenuate the interplay between conformational fluctuations, early oligomerization and amyloidosis of alpha synuclein

Aggregation of alpha synuclein has strong implications in Parkinson’s disease. The heterogeneity of folding/aggregation landscape and transient nature of the early intermediates result in difculty in developing a successful therapeutic intervention. Here we used fuorescence measurements at ensemble and single molecule resolution to study how the late and early events of alpha synuclein aggregation modulate each other.

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