Antibody-antigen binding kinetics. A model for multivalency antibodies for large antigen systems.
This work presents a theoretical analysis of the influence of multivalency of antigen on external mass transfer-limited binding kinetics to divalent antibody for biosensor applications to polycyclic-aromatic systems. Both cases are considered wherein the antigen is in solution and the antibody is either covalently or noncovalently attached to a cylindrical fiber-optic biosensor, and the antibody is in solution and the antigen is attached to the surface. Both single-step and dual-step binding processes are considered. The rate of attachment of antigen to antibody (or vice versa) is linear for the valencies (or reaction orders) analyzed in the time frame (100 min) considered. The rate of attainment of saturation levels of antigen or antibody in solution close to the surface is very rapid (within 20 min). An increase in the valency of the antigen in solution has the effect of decreasing the order of reaction (for valency, v > or = 1). An increase in the number of steps increases the order of reaction, as expected. An increase in the valency of the antigen in solution decreases the saturation level of the antigen close to the surface and the rate of antigen attachment to the antibody on the surface for all Damkohler numbers. A decrease in the diffusional limitations decreases the effect of valency (or reaction order) on saturation levels of Cs/C0. Nondimensional plots presented in the analysis help extend the analysis to different antigen-antibody systems. An increase in the valency of the antibody in solution has the effect of increasing the order of reaction (for v > 2). The effects in this case are reverse to those described earlier. For valency greater than 2, the reaction order is dependent on the antigen valency, whether it is in solution or immobilized on the surface. The general analysis presented here should be applicable to most surface reactions that involve ligand-receptor binding wherein multiple-binding sites are involved on either the receptor or the ligand.
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