Discovery and optimization of substituted oxalamides as novel heme-displacing IDO1 inhibitors

Bioorg Med Chem Lett. 2021 Feb 1:33:127744. doi: 10.1016/j.bmcl.2020.127744. Epub 2020 Dec 15.

Abstract

Since the advent of antibody checkpoint inhibitors as highly efficient drugs for cancer treatment, the development of immunomodulating small molecules in oncology has gained great attention. Drug candidates targeting IDO1, a key enzyme in tryptophan metabolism, are currently under clinical investigation in combination with PD-1/PD-L1 agents as well as with other established anti-tumor therapeutics. A ligand based design approach from hydroxyamidine 4 that aimed at heme-binding IDO1 inhibitors resulted in new compounds with moderate IDO1 potency. A hybrid structure design that made use of the linrodostat structure (2) led to oxalamide derived, heme-displacing IDO1 inhibitors with high cell-based IDO1 potency and a favorable ADME/PK profile.

Keywords: Cancer immunotherapy; Heme-displacer; IDO1; Indoleamine-2,3-dioxygenase-1; Oxalamides; Tryptophan-kynurenine-AhR-pathway.

MeSH terms

  • Amides / chemical synthesis
  • Amides / chemistry
  • Amides / pharmacology*
  • Dose-Response Relationship, Drug
  • Drug Discovery*
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Indoleamine-Pyrrole 2,3,-Dioxygenase / antagonists & inhibitors*
  • Indoleamine-Pyrrole 2,3,-Dioxygenase / metabolism
  • Molecular Structure
  • Oxamic Acid / chemical synthesis
  • Oxamic Acid / chemistry
  • Oxamic Acid / pharmacology*
  • Structure-Activity Relationship

Substances

  • Amides
  • Enzyme Inhibitors
  • IDO1 protein, human
  • Indoleamine-Pyrrole 2,3,-Dioxygenase
  • Oxamic Acid