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. 2024:2762:71-87.
doi: 10.1007/978-1-0716-3666-4_5.

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

Jason Baardsnes  1 , Béatrice Paul-Roc  2
Affiliations

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

Jason Baardsnes et al. Methods Mol Biol. 2024.

Erratum in

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).

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