Displacement experiment

I have a general question I'd like to pose regarding the analysis of ultra high affinity interactions. One such approach, when using an ITC instrument, would be to saturate one's ligand with a low affinity binder and then "displace" the low affinity binder with the high affinity binder of interest.

The solution involves solving a series of linked equilibria which results in a cubic expression for the fraction bound which is then, in turn used to analyze the apparent-K and then to extract the affinity constant for the high affinity interaction.

Is there an analagous approach that might be applied to SPR?

Hi,
I had to look in my database for some publications. There are not many on this topic and I did not find any regarding high affinity interactions. Maybe these publications are of help.
Kind regards
Arnoud

References

1. Alexander-Brett, J. M. and Fremont, D. H.; Dual GPCR and GAG mimicry by the M3 chemokine decoy receptor. J.Exp.Med. (204) 13: 3157-3172; 2007.
2. Karlsson, R.; Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors. Analytical Biochemistry (221) 1: 142-151; 1994.
3. Nieba, L., Krebber, A. and Pluckthun, A.; Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Analytical Biochemistry (234) 2: 155-165; 1996.
4. Yamniuk, A. P., Edavettal, S. C., Bergqvist, S., et al.; ABRF-MIRG benchmark study: molecular interactions in a three-component system. J Biomol Tech (23) 3: 101-14; 2012.