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Related Experiment Video

Updated: May 7, 2026

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
15:27

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

Solution-phase vs surface-phase aptamer-protein affinity from a label-free kinetic biosensor.

Camille Daniel1, Yoann Roupioz, Didier Gasparutto

  • 1Laboratoire Structure et Propriétés d'Architectures Moléculaires, UMR 5819 CEA/CNRS/UJF, Institut Nanosciences et Cryogénie, Grenoble, France.

Plos One
|September 27, 2013
PubMed
Summary

This study developed a kinetic biosensor using anti-thrombin aptamers to measure thrombin binding in real-time. The biosensor accurately quantifies thrombin, revealing distinct solution and surface binding affinities crucial for biosensor development.

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Area of Science:

  • Biomolecular Engineering
  • Biosensor Technology
  • Analytical Chemistry

Background:

  • Aptamers, selected DNA ligands, are gaining interest for therapeutic and biosensor applications.
  • Characterizing aptamer-target interactions in solution and on surfaces is critical for these applications.
  • Understanding binding kinetics is essential for optimizing biosensor performance.

Purpose of the Study:

  • To develop and validate a kinetic biosensor for real-time characterization of aptamer-target interactions.
  • To assess the kinetic parameters of anti-thrombin aptamer binding to thrombin.
  • To investigate the influence of surface immobilization on aptamer-thrombin binding affinity.

Main Methods:

  • Development of a micro-arrayed biosensor with immobilized anti-thrombin aptamers.

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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)
09:35

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

Related Experiment Videos

Last Updated: May 7, 2026

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
15:27

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)
09:35

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

  • Real-time monitoring of label-free thrombin binding using Surface Plasmon Resonance imaging.
  • Independent determination of solution-phase (KD(Sol)) and surface-phase (KD(Surf)) binding affinities.

    • Main Results:

    • Achieved sub-nanomolar limit of detection for thrombin quantification without amplification.
    • Demonstrated a linear quantification range spanning two orders of magnitude.
    • Observed distinct KD(Sol) and KD(Surf) values, influenced by aptamer grafting density.
    • Showed KD(Surf) extrapolates to KD(Sol) at low grafting densities, indicating reduced surface impact.

    Conclusions:

    • The developed kinetic biosensor provides sensitive and accurate thrombin quantification.
    • Surface immobilization significantly affects aptamer-target binding affinity compared to solution-phase interactions.
    • Aptamer grafting density is a key factor influencing surface-phase binding kinetics in biosensors.