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Related Experiment Video

Updated: Jun 25, 2026

High-throughput Confocal Imaging of Quantum Dot-Conjugated SARS-CoV-2 Spike Trimers to Track Binding and Endocytosis in HEK293T Cells
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SARS-CoV-2S-Protein-Ace2 Binding Analysis Using Surface Plasmon Resonance.

Jason Baardsnes1, Béatrice Paul-Roc2

  • 1Quality Attributes and Characterization, Human Health Therapeutics, National Research Council Canada, Montréal, QC, Canada. Jason.Baardsnes@cnrc-nrc.gc.ca.

Methods in Molecular Biology (Clifton, N.J.)
|February 5, 2024
PubMed
Summary

This study details a label-free Surface Plasmon Resonance (SPR) method to analyze the binding kinetics between the ACE2 receptor and the SARS-CoV-2 S-protein. The technique enables precise determination of binding affinity and rate constants for this crucial viral interaction.

Keywords:
Ace2Affinity (KD)AssociationBindingBinding kineticsDissociationLabel-freeSARS CoV-2S-proteinSurface plasmon resonance (SPR)

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Area of Science:

  • Biochemistry
  • Biophysics
  • Immunology

Background:

  • The interaction between the ACE2 receptor and the SARS-CoV-2 S-protein is critical for viral entry into host cells.
  • Understanding the binding kinetics of this interaction is essential for developing therapeutic interventions.
  • Label-free techniques offer advantages for studying biomolecular interactions without the need for modification or labeling of analytes.

Purpose of the Study:

  • To describe a novel Surface Plasmon Resonance (SPR) method for analyzing the ACE2-SARS-CoV-2 S-protein interaction.
  • To enable the label-free determination of binding affinity and rate constants for this interaction.
  • To establish a method for relative activity benchmarking of the S-protein.

Main Methods:

  • Utilized Surface Plasmon Resonance (SPR) for label-free analysis.
  • Employed an indirect capture method to immobilize the SARS-CoV-2 S-protein onto the SPR sensor surface.
  • Flowed monomeric ACE2 over the immobilized S-protein to measure binding kinetics.

Main Results:

  • Successfully established a method for the label-free determination of binding affinity and rate constants.
  • Demonstrated the capability to analyze the ACE2-SARS-CoV-2 S-protein interaction kinetics.
  • Developed a framework for relative activity benchmarking using S-protein capture levels and sensorgram responses.

Conclusions:

  • The described SPR method provides a robust platform for characterizing ACE2-SARS-CoV-2 S-protein interactions.
  • This technique facilitates the quantitative assessment of binding kinetics, crucial for drug discovery and development.
  • The method's adaptability allows for benchmarking of viral protein activity, aiding in understanding viral variants and therapeutic efficacy.