Binding affinity and kinetics of antibody interaction with GPCRs in native lipid environments by grating-coupled interferometry

Integral membrane proteins such as GPCRs are critical targets for therapeutic antibody drug discovery but present a host of challenges to the investigation of their biophysical properties. We demonstrate a robust approach to measuring antibody binding kinetics to GPCR drug targets expressed in crude membrane preparations and VVLPs (lipoparticles), the ability to measure antibody binding n complex matrices such as serum, as well as system stability suitable for measuring the off-rate of high affinity binding interactions as are often found in antibody-antigen systems.


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