Figure 6. In vitro binding experiments of the H27K15 mAb on various CD115 constructs. (A) Quartz Crystal Microbalance affinity profiles of the immobilized H27K15 mAb in association with hCD115_D1-D5, mCD115_D1-D5 and the hCD115_D1-D5 I1A, V8G and A17E single-point mutants. Raw data (black); model fitting (red). Kinetics parameters are reported in Table 2. (B) H^N region of the 1D ¹H NMR spectra of 250 µM peptide with the addition of increasing amounts of H27K15 antibody. Left panel, spectra of the WT (hCD115) 23-mer peptide. Right panel, spectra of the V8G mutant 23-mer peptide. (C) hydrophobicity of the interaction surface of the hCD115 and mCD115 crystal structures and the hCD115 V8G variant model based on the hCD115 crystal structure. Positions of the 4 residues of interest are indicated. Hydrophobicity plot and visualization were generated with Discovery Studio v3.5.