Determination of binding affinity and kinetics of antibody-target interactions is essential in bringing therapeutic antibodies from discovery to the market. Real-time surface-based methods are commonly used to measure complex association and dissociation at the sensor surface, but these methods have drawbacks, including long analytical run times to measure the slow dissociation rates of high-affinity interactions, and the immobilization of one interactant to the surface, which can affect kinetics. 

In this webinar, we present the benefits of in-solution equilibrium affinity experiments using Gyrolab® systems. Gyrolab systems can be used to quickly generate in-solution titration curves in relevant matrices that mimic biological systems and with interactants in their native form. An introduction to the setup and evaluation of classical in-solution equilibrium experiments for the determination of sub-nanomolar K_D values and active concentrations of interactants is discussed, along with examples of determinations of picomolar affinities for several marketed TNFa antagonists.

Key learning objectives:

• Learn how to determine sub-nanomolar KD values within an hour
• Find out how to set up in-solution equilibrium experiments using intuitive software
• Learn how results are fitted using a novel kinetic model to obtain K_D values and active interactant concentrations

• Professional groups: Ph.D. scientists, postdocs, general investigators, senior scientists, lab heads
• Research areas: Antibody engineering, antibody biotherapeutics development
• Technologies of interest: Surface plasmon resonance, antibody affinity and kinetic measurement, immunoassays