Investigate bivalent behavior with LigandTracer

Understanding binding mechanism may lead to new insights about drug efficiency and receptor structures. In a recent paper, Bondza and co-authors set up an intricate interaction study to decipher the bivalent target engagement of antibodies to B-cells.

Through real-time binding measurements with LigandTracer, it was found that the affinity and amount of anti-CD20 antibodies binding bivalently decreased at higher Ab concentrations, due to competition. The degree of bivalent binding was greater for the antibodies with high complement recruiting capability.  InteractionMap was used to investigate how the kinetics, affinity and bivalent behavior of the antibody-CD20 interaction varied with antibody concentration. Additionally, the clustering of CD20 was evaluated with our real-time proximity assay, which is relevant since both bivalent binding and Fc-Fc interactions rely on the close proximity of epitopes on the cell surface.

Please refer to the paper for more details.