Investigation of the inhibitory mechanism of apomorphine against MDM2-p53 interaction

Bioorg Med Chem Lett. 2017 Jun 1;27(11):2571-2574. doi: 10.1016/j.bmcl.2017.03.082. Epub 2017 Mar 29.

Abstract

Mirror-image screening using d-proteins is a powerful approach to provide mirror-image structures of chiral natural products for drug screening. During the course of our screening study for novel MDM2-p53 interaction inhibitors, we identified that NPD6878 (R-(-)-apomorphine) inhibited both the native l-MDM2-l-p53 interaction and the mirror-image d-MDM2-d-p53 interaction at equipotent doses. In addition, both enantiomers of apomorphine showed potent inhibitory activity against the native MDM2-p53 interaction. In this study, we investigated the inhibitory mechanism of both enantiomers of apomorphine against the MDM2-p53 interaction. Achiral oxoapomorphine, which was converted from chiral apomorphines under aerobic conditions, served as the reactive species to form a covalent bond at Cys77 of MDM2, leading to the inhibitory effect against the binding to p53.

Keywords: Apomorphine; MDM2; Michael acceptor; Mirror-image screening; Oxoapomorphine; p53.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apomorphine / chemistry
  • Apomorphine / metabolism*
  • Cell Line, Tumor
  • Humans
  • Protein Binding
  • Proto-Oncogene Proteins c-mdm2 / antagonists & inhibitors
  • Proto-Oncogene Proteins c-mdm2 / metabolism*
  • Stereoisomerism
  • Structure-Activity Relationship
  • Surface Plasmon Resonance
  • Tumor Suppressor Protein p53 / antagonists & inhibitors
  • Tumor Suppressor Protein p53 / metabolism*

Substances

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