Fast kinetic studies

Binding affinity and kinetics

MP-SPR instruments measure affinity and kinetics of the molecular binding reaction without the burdens of labelling.

The MP-SPR flow injection principle rapidly brings the sample into the measurement area (the so-called flow cell). Continuous measurements reveal how quickly molecules in the flow (analyte) bind to the surface-attached ligand molecule and how strong the interaction is. After the sample injection, buffer is again flowed into the measurement area. This measurement principle allows data to be fitted with binding models, revealing binding steady-state affinity and association and dissociation rate constants. The data analysis software contains multiple fitting models suitable for different interacting partners (e.g., small molecules, antibodies, etc.).

Fast biomolecular interaction measurements without the need for regeneration

In the traditional multi-cycle titration method (figure B), analyte samples are injected over the ligand surface at different concentrations. After sample association, the analyte is allowed to dissociate from the surface by washing with buffer. Before injecting the next analyte concentration, any remaining bound analyte is removed by injecting a suitable regeneration solution.

KineticTitration (figure A) eliminates the need for regeneration between sample concentrations and significantly reduces the time required to run a full biomolecular interaction experiment, potentially by up to half the time depending on assay type and number of concentrations. In a typical KineticTitration procedure, analyte samples are injected over the surface in a series from low to high concentration without dissociation and regeneration steps between the sample injections. The dissociation rate is measured after the last analyte sample.

See Application Note #155 for further information – small molecule drug binding to protein measured with KineticTitration.

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