Fig. 5
Surface plasmon resonance (SPR) experiments illustrating the binding strength of the recombinant antibodies to Aβ. a-d Representative sensorgrams for the recombinant antibodies’ binding to immobilized Aβ1-42 protofibrils. Three-fold dilution series of the recombinant antibodies was used to make single cycle kinetic measurements (1.23, 3.7, 11.1, 33.3 and 100 nM). The dissociation rate constants (kd) with standard deviations for the four antibodies were calculated using a one-to-one kinetic model. Lower rate of dissociation from protofibrils is measured in Tetra-RmAb158 (c) and Hexa-RmAb158 (d). e–h Representative sensor grams for Aβ1-40 monomers binding to immobilized recombinant antibodies. Two-fold dilution series of Aβ1-40 monomers used (4000, 2000, 1000, 500 and 250 nM). Lines were fitted using steady state kinetic model. The four antibodies exhibited similar steady-state affinity with KD values in the micromolar range. Results are generated from two to five repetitive experiments