Selective Degradation of Polo-like Kinase 1 by a Hydrophobically Tagged Inhibitor of the Polo-Box Domain

Angew Chem Int Ed Engl. 2018 Dec 21;57(52):17043-17047. doi: 10.1002/anie.201809640. Epub 2018 Nov 27.

Abstract

Hydrophobic tagging (HT) of bioactive compounds can induce target degradation via the proteasomal pathway. The first application of hydrophobic tagging to an existing inhibitor of protein-protein interactions is now presented. We developed Poloxin-2HT by fusing an adamantyl tag to Poloxin-2, an inhibitor of the polo-box domain of the protein kinase Plk1, which is a target for tumor therapy. Poloxin-2HT selectively reduced the protein levels of Plk1 in HeLa cells and had a significantly stronger effect on cell viability and the induction of apoptosis than the untagged PBD inhibitor Poloxin-2. The change in cellular phenotype associated with the addition of the hydrophobic tag to Poloxin-2 demonstrated that Poloxin-2HT targets Plk1 in living cells. Our data validate hydrophobic tagging of selective inhibitors of protein-protein interactions as a novel strategy to target and destroy disease-relevant proteins.

Keywords: apoptosis; inhibitors; mitotic arrest; protein degradation; protein-protein interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / antagonists & inhibitors*
  • Cell Cycle Proteins / metabolism
  • Cell Survival / drug effects
  • Dose-Response Relationship, Drug
  • HeLa Cells
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Structure
  • Polo-Like Kinase 1
  • Protein Domains / drug effects
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / pharmacology*
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins / antagonists & inhibitors*
  • Proto-Oncogene Proteins / metabolism
  • Structure-Activity Relationship

Substances

  • Cell Cycle Proteins
  • Protein Kinase Inhibitors
  • Proto-Oncogene Proteins
  • Protein Serine-Threonine Kinases