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. 2021 Jun 18;12:3752. doi: 10.1038/s41467-021-24039-2

Fig. 3. Effect of PSMα3 on in vitro αS amyloid fibrillation.

Fig. 3

a Inhibition of α-synuclein (αS) amyloid aggregation as measured by Th-T fluorescence after 32 h incubation in the presence of equimolar concentrations of PSMα3, SynuClean-D (SC-D), and dPSMα3. **** p < 0.0001 relative to untreated αS (unpaired two-tailed t tests (Welch-corrected)). Data were expressed as mean ± s.e.m (n = 6 and 3 independent experiments for untreated and treated conditions respectively). NS no significant, p = 0.23. b Aggregation kinetics of 70 μM αS and titration of the inhibitory activity of PSMα3 at different concentrations: 35 μM (green), 14 μM (orange), 7 μM (blue), 3.5 μM (gray) and in the absence of PSMα3 (black). Data were expressed as mean ± s.e.m (n = 9 independent experiments). c Representative TEM micrographs of αS aggregated for 32 h in the absence (left) and presence of an equimolar concentration of PSMα3 (right) that came from two independent replicates. d Representative TEM micrographs illustrating the morphological differences between low-molecular weight aggregates of αS after 12 h of incubation in absence (left) and presence of PSMα3 (right). Results are consistent in two independent replicates. Inset shows an annular oligomer at high magnification.