Figure 7: Sequence specificity of small molecule-mediated inhibition of vesicle-bound αSyn amyloid formation. | Nature Communications

Figure 7: Sequence specificity of small molecule-mediated inhibition of vesicle-bound αSyn amyloid formation.

From: Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation

Figure 7

(a) Fibrillization kinetics of wt αSyn and its mutants in the presence of a ~12.5mM concentration of SUVs. Shown is the normalized ThT intensity for increasing times of incubation in aggregation-prone conditions. The concentration of αSyn was 100 μM and the molar ratio of PcTS to protein was 15:1. The blue line shows the fibrillization kinetics of wt αSyn in the absence of PcTS. In the presence of PcTS, wt αSyn (black) does not form ThT-positive fibrils. Removing one aromatic residue decreases the PcTS-inhibitory effect (green and red lines). Removal of both Y39 and F94 (purple line) largely abolishes the PcTS-mediated aggregation inhibition. The circles represent the average ThT intensity of at least three different experiments normalized against their respective maximum values. (b) ThT fluorescence after 6 days of aggregation. The error bars represent the s.e. of at least three different samples.

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