Figure 2
From: Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β
Surface plasmon resonance analysis of the binding of anti-Aβ antibody Fab fragments to Aβ1-40-biotin immobilized on a biotin-capture sensor chip surface. Sensorgrams for (a) chaducanumab Fab (0.31, 0.62, 1.25, 2.5, 5, 10, 20 and 40 μM), (b) chgantenerumab Fab (5, 14, 41, 120, 370 and 1,100 nM), (c) 3D6 Fab (0.5, 1.5, 5, 14, 41, 120, 370 and 1,100 nM), and (d) m266 Fab (0.5, 1.5, 5, 14, 41, 120, 370 and 1,100 nM) are shown (grey curves) with corresponding fits to a 1:1 binding model (red curves). Fabs were injected over an Aβ1-40-biotin coated sensor chip for 2 min in (a) and 3 min in (b–d), where the rising response describes the approach to steady state binding and beyond which the response drops due to dissociation of the Fabs. In (a), the binding and dissociation kinetics could not be determined, but the equilibrium dissociation constant was evaluated from fitting the steady state binding response (inset). Calculated kinetics and affinity constants are listed in Table 2.
