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Related Experiment Video

Updated: Jun 22, 2026

Determination of the Excitation and Coupling Rates Between Light Emitters and Surface Plasmon Polaritons
07:39

Determination of the Excitation and Coupling Rates Between Light Emitters and Surface Plasmon Polaritons

Published on: July 21, 2018

An indirect method to measure trimerization constants using surface plasmon resonance.

M Mattu1, C Bendtsen, G Barbato

  • 1Biotechnology, IRBM, 00040 Pomezia, Italy.

Analytical Biochemistry
|June 16, 2009
PubMed
Summary
This summary is machine-generated.

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Surface plasmon resonance precisely measured kinetic binding constants to indirectly determine the trimerization constant (Kd) of the chimeric protein IZN-23. This method offers a novel approach for evaluating protein complex stability.

Area of Science:

  • Biochemistry
  • Protein Engineering
  • Biophysical Chemistry

Background:

  • Chimeric proteins like IZN-23, derived from isoleucine zippers and HIV-1 gp41, present unique structural and binding properties.
  • Understanding the thermodynamic stability, specifically the trimerization constant (Kd), is crucial for characterizing such engineered proteins.

Purpose of the Study:

  • To indirectly evaluate the thermodynamic dissociation trimerization constant (Kd) of the designed chimeric protein IZN-23.
  • To demonstrate the utility of surface plasmon resonance (SPR) in assessing protein complex formation kinetics.

Main Methods:

  • Utilized surface plasmon resonance (SPR) to measure kinetic binding constants.
  • Employed two monoclonal antibodies (mAbs) with differential binding kinetics to monomeric and trimeric IZN-23.

More Related Videos

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: Jun 22, 2026

Determination of the Excitation and Coupling Rates Between Light Emitters and Surface Plasmon Polaritons
07:39

Determination of the Excitation and Coupling Rates Between Light Emitters and Surface Plasmon Polaritons

Published on: July 21, 2018

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

  • Developed a data analysis strategy to derive Kd from observed off-rate kinetic values.

    • Main Results:

    • Successfully exploited SPR to indirectly determine the trimerization constant (Kd) of IZN-23.
    • Demonstrated that mAbs exhibit distinct off-rates for monomeric versus trimeric IZN-23.
    • Presented a detailed data analysis approach for extracting trimerization constants from kinetic data.

    Conclusions:

    • The study validates SPR as a powerful tool for indirectly assessing thermodynamic constants of protein complex formation.
    • The developed methodology provides a framework for evaluating the stability of engineered protein assemblies.
    • Highlights the potential application of this technique in various scientific fields for protein characterization.