Fig. 2: Structural characterization of the binding interaction between SK-129 and αS.
From: Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly
a–d Overlay of 2D HSQC (1H, 15N) NMR spectra of 70 µM uniformly 15N-labeled αS in the absence (black) and presence (yellow) of SK-129 at an equimolar ratio. The largest attenuation in the volume of the backbone amide residue NMR signals are highlighted and assigned, which includes αS segments from 6–12 (a), 15–23 (b), 36–45 (c), and 48–53 (d). The change in the volume of amide backbone residue peaks of αS was compared between SK-129 and a molecular chaperone SecB (*, red) and the pronounced changes were observed in segments 6–12 (a) and 36–45 (b). e Graphical presentation of the changes in the chemical shifts of the backbone amide residue peaks of 15N-labeled αS (70 µM) in the presence of SK-129 at an equimolar ratio. The colored sequences are the potential binding sites of SK-129 on αS. CD-based characterization of the aggregation kinetics of 35 µM αS in the absence (f) and presence (g) of SK-129 at an equimolar ratio. The spectra were recorded for 7 days. Source data are provided as a Source Data file.
