SARS-CoV-2S-Protein-Ace2 Binding Analysis Using Surface Plasmon Resonance

Abstract

Surface plasmon resonance (SPR) allows for the label-free determination of the binding affinity and rate constants of bimolecular interactions. Here, we describe the method used for the analysis of the Ace2-SARS-CoV2 S-protein interaction using indirect capture of the S-protein onto the SPR surface, and flowing monomeric Ace2. This method will allow for the determination of the rate constants for affinity, with additional analysis that is achievable using S-protein capture levels in conjunction with the sensorgram response for relative activity benchmarking.

Keywords: Ace2; Affinity (KD); Association; Binding; Binding kinetics; Dissociation; Label-free; SARS CoV-2S-protein; Surface plasmon resonance (SPR).