Discovery of dihydroisoquinolinone derivatives as novel inhibitors of the p53-MDM2 interaction with a distinct binding mode

Bioorg Med Chem Lett. 2015 Sep 1;25(17):3621-5. doi: 10.1016/j.bmcl.2015.06.058. Epub 2015 Jun 23.

Abstract

Blocking the interaction between the p53 tumor suppressor and its regulatory protein MDM2 is a promising therapeutic concept under current investigation in oncology drug research. We report here the discovery of the first representatives of a new class of small molecule inhibitors of this protein-protein interaction: the dihydroisoquinolinones. Starting from an initial hit identified by virtual screening, a derivatization program has resulted in compound 11, a low nanomolar inhibitor of the p53-MDM2 interaction showing significant cellular activity. Initially based on a binding mode hypothesis, this effort was then guided by a X-ray co-crystal structure of MDM2 in complex with one of the synthesized analogs. The X-ray structure revealed an unprecedented binding mode for p53-MDM2 inhibitors.

Keywords: MDM2; Protein–protein interaction inhibitors; p53.

MeSH terms

  • Crystallography, X-Ray
  • Humans
  • Isoquinolines / chemistry*
  • Isoquinolines / pharmacology*
  • Molecular Docking Simulation
  • Protein Binding / drug effects
  • Protein Interaction Maps / drug effects*
  • Proto-Oncogene Proteins c-mdm2 / antagonists & inhibitors
  • Proto-Oncogene Proteins c-mdm2 / metabolism*
  • Structure-Activity Relationship
  • Tumor Suppressor Protein p53 / antagonists & inhibitors
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • Isoquinolines
  • Tumor Suppressor Protein p53
  • Proto-Oncogene Proteins c-mdm2