Key Takeaways

  • Using neonatal Fc receptor (FcRn) as a model system, the versatility of the LSA is demonstrated by measuring binding in three different assay strategies
  • Kinetic affinity, steady-state affinity, and IC50 potency values were all obtained using the same ligand array
  • Multiple conditions and controls, all in triplicate, were included due to the high-throughput nature of the LSA
  • The capability to conduct potency assays on the LSA highlights new opportunities for leveraging high-throughput surface plasmon resonance (HT-SPR) in drug discovery and development


Potency assays have wide applicability in life science research and development. For therapeutic drug candidates, they are essential across the spectrum of discovery and into development. While many potency assay formats are endpoint in nature, such as enzyme-linked immunosorbent assay (ELISA), there are examples where real-time, label-free technologies have been used to determine potency1. Here we demonstrate how potency assays can be leveraged as part of an overall characterization strategy via HT-SPR using the Carterra LSA. The versatility of the LSA enables researchers to easily adapt to this assay format in conjunction with more commonly used techniques of measuring binding affinity. Additionally, HT-SPR with the LSA presents opportunities to measure up to hundreds of interactions simultaneously, allowing for inclusion of varied assay conditions, controls, and replicates not typically feasible with other technologies. Using FcRn as a model system, this application note explores a workflow to characterize kinetic affinity, steady state affinity, and potency in a series of experiments that can be completed in a single day.

Posted by Noah T. Ditto