Identification of Substituted Naphthotriazolediones as Novel Tryptophan 2,3-Dioxygenase (TDO) Inhibitors through Structure-Based Virtual Screening

J Med Chem. 2015 Oct 8;58(19):7807-19. doi: 10.1021/acs.jmedchem.5b00921. Epub 2015 Sep 16.

Abstract

A structure-based virtual screening strategy, comprising homology modeling, ligand-support binding site optimization, virtual screening, and structure clustering analysis, was developed and used to identify novel tryptophan 2,3-dioxygenase (TDO) inhibitors. Compound 1 (IC50 = 711 nM), selected by virtual screening, showed inhibitory activity toward TDO and was subjected to structural modifications and molecular docking studies. This resulted in the identification of a potent TDO selective inhibitor (11e, IC50 = 30 nM), making it a potential compound for further investigation as a cancer therapeutic and other TDO-related targeted therapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Databases, Chemical
  • Drug Evaluation, Preclinical / methods*
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Ligands
  • Molecular Docking Simulation
  • Structure-Activity Relationship*
  • Triazoles / chemistry
  • Tryptophan Oxygenase / antagonists & inhibitors*
  • Tryptophan Oxygenase / chemistry
  • Tryptophan Oxygenase / metabolism

Substances

  • Enzyme Inhibitors
  • Ligands
  • Triazoles
  • Tryptophan Oxygenase