Fig. 6: α-Syn uses its acidic C-terminal to bind with CD4 D1, CAR D1, and CAR D1_Mut.
From: Design of Ig-like binders targeting α-synuclein fibril for mitigating its pathological activities
Electrostatic surface of the representative complex structure of α-syn115–135-CD4 D1 (a), α-syn115–135-CAR D1 (b), and α-syn115–135-CAR D1_Mut (d) which were predicted by AlphaFold 3. The complex interfaces were zoomed in (bottom). Salt bridges are highlighted in orange lines and hydrogen bonds are in dark gray lines. c Violin plots of ΔΔG (Gibbs free energy change) and ΔΔG/ΔSASA (ΔΔG per unit change in solvent accessible surface area) for three complexes, each calculated from 200 trials. (REU, Rosetta Energy Unit). One-way ANOVA followed by Tukey’s post-hoc test. Data shown are mean ± s.d. ****p < 0.0001. All p values were < 0.0001. e Binding kinetics of CAR D1_Mut with α-syn monomer (left) and α-syn PFF (right) measured by BLI assay. The association and dissociation profiles were divided by a vertical dash. Ig-like binders were fixed to the sensors, and the 5 concentrations of α-syn monomer (left) and PFF (right) used are indicated. Source data are provided as a Source Data file.
