Optimizing kinetics assay to avoid avidity effects

In this application note, Sartorius discusses the importance of biosensor-based real-time label-free interaction analysis using bio-layer interferometry (BLI) in the research and development of biologics targeting specific binding partners. The note emphasizes the characterization of binding properties such as kinetics and affinity parameters during the screening process, which enables the selection of lead candidates for further development. Additionally, the application note highlights the significance of understanding the differences between affinity and avidity in assay design, including considerations of assay orientation, valency, ligand surface density, and non-specific binding. By addressing these factors, a robust assay design can minimize artifacts and ensure the accurate determination of binding kinetics and affinity, ultimately facilitating the generation of desired assay parameters for interacting molecules.