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Targeting NOX2 with Bivalent Small-Molecule p47phox-p22phox Inhibitors.

Jie Zang1, Felix Peters1, Yves Cambet2

  • 1Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark.

Journal of Medicinal Chemistry
|October 19, 2023
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Summary

Researchers developed potent small-molecule inhibitors targeting the p47phox subunit of Nicotinamide adenine dinucleotide phosphate oxidase isoform 2 (NOX2). These inhibitors show submicromolar binding affinities and cellular activity, demonstrating NOX2 as a viable drug target.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Molecular Biology

Background:

  • Nicotinamide adenine dinucleotide phosphate oxidase isoform 2 (NOX2) generates reactive oxygen species (ROS), crucial for signaling but implicated in oxidative stress and inflammation.
  • The p47phox subunit's interaction with p22phox is vital for NOX2 activation, making p47phox a key drug target.

Purpose of the Study:

  • To systematically optimize bivalent small-molecule inhibitors targeting the p47phox-p22phox interaction.
  • To identify novel compounds with enhanced binding affinities and cellular activity against NOX2.

Main Methods:

  • Fragment-based drug discovery and lead optimization of 2-aminoquinoline derivatives.
  • Exploration of linker types, positioning, and substituents for bivalent inhibitors.
  • Biophysical methods to characterize compound binding modes.
  • Assessment of cellular activity of optimized compounds.

Main Results:

  • Identification of novel bivalent small molecules with submicromolar binding affinities to p47phox.
  • Demonstration of cellular activity for the optimized NOX2 inhibitors.
  • Characterization of the bivalent binding mode using biophysical techniques.

Conclusions:

  • p47phox can be effectively targeted by potent small-molecule inhibitors.
  • Optimized bivalent compounds represent promising therapeutic agents for diseases involving NOX2 hyperactivity.
  • This study validates NOX2 as a druggable target through inhibition of its subunit interactions.