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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Extending ITC to Kinetics with kinITC.

Philippe Dumas1, Eric Ennifar1, Cyrielle Da Veiga1

  • 1Biophysics & Structural Biology Team, IBMC, UPR9002-CNRS, University of Strasbourg, Strasbourg, France.

Methods in Enzymology
|January 23, 2016
PubMed
Summary
This summary is machine-generated.

Isothermal titration calorimetry (ITC) can now reveal reaction kinetics, not just thermodynamics, with the kinITC method. This technique accurately measures binding rates (kon) for biological interactions, offering an alternative to surface plasmon resonance.

Keywords:
Biological calorimetryEquilibration time curveITCKineticsMicrocalorimetrykinITC

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Area of Science:

  • Biophysical Chemistry
  • Biochemistry
  • Chemical Kinetics

Background:

  • Isothermal titration calorimetry (ITC) is traditionally used for thermodynamic characterization.
  • The biological field has largely overlooked ITC's potential for kinetic studies.
  • Surface plasmon resonance (SPR) is the dominant technique for kinetic analysis in biology.

Purpose of the Study:

  • To demonstrate the kinetic capabilities of ITC using a novel extension called kinITC.
  • To provide a theoretical framework for applying ITC to second-order reactions (A+B Ω C).
  • To present a simplified kinITC-Equilibration Time Curve (ETC) method for kinetic parameter determination.

Main Methods:

  • Development and theoretical basis of kinITC for kinetic analysis.
  • Implementation of a simplified kinITC-ETC method using automatic determination of injection endpoints.
  • Experimental validation of kinITC by comparing results with Surface Plasmon Resonance (SPR) data.

Main Results:

  • ITC successfully recovered kinetic information, challenging its traditional thermodynamic role.
  • The kinITC-ETC method determined kon values across a broad range (10^3 to 0.5×10^6 M⁻¹s⁻¹).
  • Experimental results demonstrated good agreement with SPR data, validating the kinITC approach.

Conclusions:

  • kinITC unlocks the kinetic potential of ITC for biological and chemical studies.
  • The kinITC-ETC method provides a robust and accessible approach for measuring reaction kinetics.
  • AFFINImeter software now incorporates these kinITC procedures, facilitating their application.