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Chemical force microscopy with active enzymes.

M Fiorini1, R McKendry, M A Cooper

  • 1Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.

Biophysical Journal
|April 28, 2001
PubMed
Summary
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Researchers measured adhesion forces between an enzyme-coated atomic force microscope tip and an ATP mimic. Specific interactions, not general binding, were responsible for the observed forces, paving the way for new screening methods.

Area of Science:

  • Biophysics
  • Biochemistry
  • Surface Science

Background:

  • Atomic Force Microscopy (AFM) is a powerful tool for probing molecular interactions.
  • Enzyme immobilization on surfaces is crucial for developing biosensors and diagnostic tools.
  • Understanding specific enzyme-ligand interactions is key to drug discovery and molecular recognition.

Purpose of the Study:

  • To quantify adhesion forces between shikimate kinase and an ATP mimic using AFM.
  • To investigate the specificity of the enzyme-surface interactions.
  • To establish a foundation for a chemical force microscopy-based screening methodology.

Main Methods:

  • Utilized an atomic force microscope (AFM) with a tip functionalized with shikimate kinase.
  • Immobilized an ATP mimic on a gold surface for binding experiments.

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  • Performed competitive binding assays with various ligands in solution to assess interaction specificity.

    • Main Results:

    • Measured adhesion forces between the enzyme-modified AFM tip and the immobilized ATP mimic.
    • Demonstrated that the observed adhesion forces are primarily due to specific shikimate kinase-ATP mimic interactions.
    • Competitive binding experiments confirmed the specificity of the observed molecular recognition event.

    Conclusions:

    • The study successfully measured specific adhesion forces between shikimate kinase and an ATP mimic.
    • These findings validate the use of chemical force microscopy for studying enzyme-ligand interactions.
    • The developed methodology shows promise for high-throughput screening of molecular interactions.