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Related Experiment Videos

Lectin-carbohydrate affinity measured using a quartz crystal microbalance.

Kateryna Lebed1, Andrzej J Kulik, László Forró

  • 1The Henryk Niewodniczański Institute of Nuclear Physics, Polish Academy of Sciences, Radzikowskiego 152, 31-342 Kraków, Poland. kateryna.lebed@ifj.edu.pl

Journal of Colloid and Interface Science
|March 15, 2006
PubMed
Summary

This study quantifies molecular interactions using quartz crystal microbalance, revealing how immobilization affects binding kinetics. Findings highlight the influence of molecule orientation on association equilibrium constants for concanavalin A and carboxypeptidase Y.

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Area of Science:

  • Biochemistry
  • Surface Science
  • Analytical Chemistry

Background:

  • Molecular interactions are typically characterized in solution.
  • Immobilizing molecules on substrates can alter binding kinetics.
  • Concanavalin A and carboxypeptidase Y form a lectin-carbohydrate complex.

Purpose of the Study:

  • To determine association constants for immobilized concanavalin A and carboxypeptidase Y.
  • To investigate the impact of immobilization on binding kinetics.
  • To demonstrate quartz crystal microbalance utility for studying molecular association.

Main Methods:

  • Quartz crystal microbalance (QCM) measurements in liquid.
  • Immobilization of concanavalin A on a gold electrode.
  • Addition of carboxypeptidase Y to a buffer solution.

Related Experiment Videos

  • Saturation binding experiments.

    • Main Results:

    • Association equilibrium constant: (0.59±0.01)×10⁶ M⁻¹.
    • Association rate constant: (5.6±0.1)×10⁴ M⁻¹s⁻¹.
    • Saturation binding yielded an association constant of (2.7±0.02)×10⁶ M⁻¹.

    Conclusions:

    • Immobilization and molecule orientation influence association equilibrium constants.
    • Quartz crystal microbalance is effective for real-time detection and evaluation of molecular association.
    • The study provides quantitative data on lectin-carbohydrate interactions.