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Assaying Protein Kinase Activity with Radiolabeled ATP
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A Wild-Type Nanopore Sensor for Protein Kinase Activity.

Fu-Na Meng1, Yi-Lun Ying1,2, Jie Yang1

  • 1School of Chemistry and Molecular Engineering , East China University of Science and Technology , Shanghai , 200237 , P. R. China.

Analytical Chemistry
|June 27, 2019
PubMed
Summary

A novel nanopore sensor detects protein kinase activity without labeling. This method enables sensitive kinase detection, inhibitor screening, and real-time monitoring for drug discovery and diagnostics.

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Area of Science:

  • Biochemistry
  • Nanotechnology
  • Enzymology

Background:

  • Protein kinases regulate crucial cellular processes.
  • Accurate kinase activity detection is vital for research and diagnostics.
  • Existing methods often require complex procedures and modifications.

Purpose of the Study:

  • To develop a novel, simplified method for detecting kinase activity.
  • To enable label-free, real-time monitoring of kinase-catalyzed phosphorylation.
  • To create a versatile sensor for enzyme activity screening and drug discovery.

Main Methods:

  • Utilized a wild-type aerolysin nanopore for label-free detection.
  • Employed selective capture of phosphopeptides within the nanopore.
  • Integrated an internal standard method for quantitative analysis.
  • Demonstrated kinase inhibitor screening and cell lysate analysis.

Main Results:

  • Achieved a detection limit of 0.005 U/μL for protein kinase A.
  • Observed a dose-dependent response of phosphopeptide events with kinase activity.
  • Successfully monitored kinase activity in cell lysates.
  • Showcased real-time, single-molecule phosphorylation monitoring.

Conclusions:

  • The developed nanopore sensor offers a sensitive and efficient platform for kinase activity detection.
  • This method facilitates kinase inhibitor screening and diagnostics.
  • The sensor's versatility extends to other enzymes altering substrate charge, broadening its applicability.