Critical Reagent Characterization on Gyrolab using Solution Based Affinity Module: A Case Study

Last updated: 26th February, 2018

Other than specificity, the affinity (KD) of an antibody reagent binding to a drug target is the most important property that drives PK, ADA and NAb assay performance. Kinetic properties (Kon and Koff) may be determined to calculate KD using surface-based methods, such as Biacore or Octet. Alternatively, equilibrium-based methods may be utilized by determining concentrations of binding partners in solution. Gyrolab was evaluated as a tool to measure equilibrium solution-based KD of critical reagents (Fab and mouse Mab) binding to various human Mab drug targets and the data compared to kinetic-based surface methodologies, such as Octet and Biacore.

In addition, Gyrolab affinity assay data was evaluated using KinExa software to compare and establish a global fit for a more accurate KD measurement. Differences in affinity measurements were found across methodologies and can be attributed to a variety of factors, including avidity, valency of interactants, assay format and matrix effects. Gyrolab is a useful tool to characterize high affinity assay reagents that are beyond the detection limits for Octet or Biacore, and affords automation, short assay/contact time, small reagent volumes and unmodified interactants.

  • Gyrolab solution-based method for measuring KD values in the low pM range
  • Feasibility of Gyrolab to characterize reagent affinity to Mab drug and comparison to alternate methods (Biacore and Octet)
  • Data fit comparison between KinExa and Gyrolab software
  • Case study: high affinity interaction between 2 Mabs (Low pM KD Range)

Alison Joyce, Senior Principal Scientist, Biomedicine Design, Discovery Bioanalytical and Critical Reagent Group, Pfizer Inc. Alison will answer your questions live during the broadcast!

Thursday 22nd March, 2018

11am – 12pm EDT



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