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Probing protein binding spectra with Fourier microfluidics.

C H Mastrangelo1, L D Williams, T Ghosh

  • 1Electrical Engineering and Bioengineering Departments, University of Utah, Salt Lake City, UT 84112, USA. carlos.mastrangelo@utah.edu

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference
|November 25, 2010
PubMed
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This study introduces a microfluidic chip for Fourier transform analysis of biochemical interactions. The technology enables precise measurement of binding kinetics, offering a new tool for chemical analysis.

Area of Science:

  • Biochemistry
  • Microfluidics
  • Analytical Chemistry

Background:

  • Microfluidic chip technology advancements allow for the development of chemical spectrum analyzers.
  • These analyzers can investigate binding interactions between various chemical entities.
  • Fourier transform measurements offer a powerful method for analyzing dynamic biochemical processes.

Purpose of the Study:

  • To implement a microfluidic chip specifically designed for Fourier transform measurements of biochemical interactions.
  • To demonstrate the capability of this chip in probing binding kinetics.
  • To validate the technique using a model biochemical system.

Main Methods:

  • Development of a microfluidic chip integrating a chemical signal generator, flow cell, and binding sensor surface.

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  • Generation of periodic protein plugs in solution flowing through the cell to induce cycles of association and dissociation.
  • Optical measurement of sensor activity using surface plasmon resonance (SPR) imaging to capture the phasor response.

    • Main Results:

    • The microfluidic chip successfully generated periodic association and dissociation cycles of proteins to a functionalized gold surface.
    • Surface plasmon resonance (SPR) imaging provided optical measurements of the sensor's phasor response.
    • Analysis of the transfer function revealed a dominant pole at 10.2 mHz, yielding association and dissociation constants for carbonic anhydrase-II and its ligand.

    Conclusions:

    • The implemented microfluidic chip is suitable for Fourier transform measurements of biochemical interactions.
    • The technique allows for the determination of binding kinetics, specifically association and dissociation constants.
    • This technology offers a novel approach for analyzing chemical and biochemical binding events with high precision.