S. A. Bobrovnik, M. O. Demchenko, S. . Komisarenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: s-bobrov@bk.ru

Theoretical aspects of the affinity evaluation for the interaction between bivalent receptors (or antibodies) and corresponding ligands (or antigens) are considered. It was shown that the ligand presen­ce in the solution at the stage when the receptor dissociation occurs leads to the increase of the affinity evaluation accuracy. We demon­strated that the analysis of the dissociative curve of the receptor from the chip is not necessary for affinity determination; the analysis of associative curve is sufficient for this purpose. We also suggested a new approach for evaluating the affini­ty of bivalent receptors (or antibodies) when these reagents are present in the studied solution and the correspondent ligand (or antigen) is immobilized on the chip.

Keywords: affinity of interaction, equilibrium constant, method of surface plasmon resonance, rate constants