Structure-activity relationship study of small-molecule inhibitor of Atg12-Atg3 protein-protein interaction

Bioorg Med Chem Lett. 2024 Nov 1:112:129939. doi: 10.1016/j.bmcl.2024.129939. Epub 2024 Aug 31.

Abstract

Autophagy is a catabolic process that was described to play a critical role in advanced stages of cancer, wherein it maintains tumor cell homeostasis and growth by supplying nutrients. Autophagy is also described to support alternative cellular trafficking pathways, providing a non-canonical autophagy-dependent inflammatory cytokine secretion mechanism. Therefore, autophagy inhibitors have high potential in the treatment of cancer and acute inflammation. In our study, we identified compound 1 as an inhibitor of the ATG12-ATG3 protein-protein interaction. We focused on the systematic modification of the original hit 1, a casein kinase 2 (CK2) inhibitor, to find potent disruptors of ATG12-ATG3 protein-protein interaction. A systematic modification of the hit structure led us to a wide plethora of compounds that maintain its ATG12-ATG3 inhibitory activity, which could act as a viable starting point to design new compounds with diverse therapeutic applications.

Keywords: Autophagy; Autophagy inhibition; Protein–protein interaction; Small molecule.

MeSH terms

  • Autophagy / drug effects
  • Autophagy-Related Proteins* / antagonists & inhibitors
  • Autophagy-Related Proteins* / metabolism
  • Casein Kinase II / antagonists & inhibitors
  • Casein Kinase II / metabolism
  • Dose-Response Relationship, Drug
  • Humans
  • Molecular Structure
  • Protein Binding
  • Small Molecule Libraries* / chemical synthesis
  • Small Molecule Libraries* / chemistry
  • Small Molecule Libraries* / pharmacology
  • Structure-Activity Relationship

Substances

  • Small Molecule Libraries
  • Autophagy-Related Proteins
  • Casein Kinase II