Fig. 5: CD4 D1 and CAR D1 interact with the C-terminal of α-syn.
From: Design of Ig-like binders targeting α-synuclein fibril for mitigating its pathological activities
Overlaid 2D HSQC spectra of 15N-labeled α-syn monomer alone (black) and that titrated by CD4 D1 (a, left) and CAR D1 (b, left) at a molar ratio of 1:1 (α-syn:CD4 D1/CAR D1). Representative residues with significant CSDs were zoomed in on the right. c, d Calculated CSDs of 15N-labeled α-syn monomer titrated by CD4 D1 from (a) and by CAR D1 from (b). The black dashed lines indicate the residues with CSDs > 0.01 ppm (c) and 0.005 ppm (d), respectively. The binding kinetics of CD4 D1 (e) and CAR D1 (f) with α-syn100 monomer (left) and α-syn100 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-syn100 monomer (left) and PFF (right) used are indicated. N.D., not detected. Source data are provided as a Source Data file.
