Extended Data Fig. 2: Binding affinities of ligands to α-syn fibrils measured by fluorescent binding saturation curves.
From: Structural mechanism for specific binding of chemical compounds to amyloid fibrils
a, Differential fluorescent spectra of 50 μM ligands in the presence and absence of 50 μM α-syn fibrils. Differential fluorescence signal intensities (Ligandbound - Ligandfree) are shown as mean ± s.d., n = 3 independently prepared samples. The chemical structures of the ligands are shown. b, The fluorescent binding curves of the ligands to α-syn fibrils measured at the excited and maximum emission wavelengths in (a). 1 µM of α-syn fibrils were added. Data are shown as mean ± s.d., n = 3 independent samples. The curves were analyzed by nonlinear regression with a saturation binding equation. c, The fitting results of (b). Binding affinity KD is the concentration of ligand required to reach half-maximal binding, and h is the Hill coefficient. Bmax is the maximal binding signal.
