Fig. 3: SK-129-based mutation study to delineate the role of αS sequences in aggregation.
From: Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly
a A schematic of the design of αS variants where “x” represents the deleted sequence from the WT αS. b–e The fits for the FP titrations to determine the binding affinities between 10 µM SK-129F and αS variants (inset). The data were expressed as mean and the error bars report the S.D. (n = 3 independent experiments). f–j ThT fluorescence-based aggregation kinetic profiles of 100 µM αS variants in the absence (closed circle) and presence (open circle) of SK-129 at an equimolar ratio. The circles represent the average ThT intensity of three different experiments. The data were expressed as mean and the error bars report the S.D. (n = 3 independent experiments). k–o TEM images of αS variants (100 µM) after aggregated them for seven days. p–t CD spectra of monomeric (light color, monomer) and the aggregated (dark color, 7 days) states of αS variants (35 µM). The same aggregated samples of αS variants were used for both CD and TEM images. u–y Aggregation profiles of 100 µM αS variants catalyzed by preformed fibers of WT αS (10 µM in monomeric unit) in the absence (close circle) and presence (open circle) of SK-129 at an equimolar ratio. The data were expressed as mean and the error bars report the S.D. (n = 3 independent experiments). Source data are provided as a Source Data file.
