Structural and Functional Insights into the Malaria Parasite Moving Junction Complex
Figure 6
Surface Plasmon Resonance studies of peptide R1 binding to PfAMA1 mutants 3D7mut and Dico3.
(A). Left - sensorgrams, showing R1 (analyte) binding to PfAMA1 3D7mut (immobilized). R1 concentrations are indicated for each curve (µM). Right - the variation in percentage of bound sites (deduced from the steady-state response) with respect to analyte concentration. (B). Left - sensorgrams, showing R1 (analyte) binding to Dico3 (immobilized), with R1 concentrations indicated. Right - the variation in percentage of bound sites (deduced from the steady-state response) with respect to analyte concentration. The equilibrium dissociation constant KD derived from the steady state binding curves is 15.2 µM for 3D7mut and 22.3 µM for Dico3.