The matrix effects on kinetic rate constants of antibody–antigen interactions reflect solvent viscosity

摘要: Abstract This study describes the influence of different matrices on two model antibody–antigen interactions; that between β2microglobulin and anti β2microglobulin, rabbit mouse Fc fragment (RAMFc) with IgG. The investigated were; phosphate-buffered saline pH 7.4 containing 0.05% Tween 20 detergent, horse serum, a 50:50 mixture saline/Tween four glycerol solutions differing concentrations. A recently developed optical biosensor, IAsys™, was used to monitor interactions in real-time provide precise determinations kass, kdiss KA values. results show rates association dissociation for antibody:antigen models are significantly affected by surrounding matrix. Glycerol known viscosity as matrix both this effect is attributable opposed proteins present has also been shown have an apparent upon overall equilibrium/affinity constant interaction, measurements tending increase viscosity. significant effects kinetic rate constants here important implications use immunoassays where non-equilibrium made serum matrices.