Identification of potent Yes1 kinase inhibitors using a library screening approach

Bioorg Med Chem Lett. 2013 Aug 1;23(15):4398-403. doi: 10.1016/j.bmcl.2013.05.072. Epub 2013 May 29.

Abstract

Yes1 kinase has been implicated as a potential therapeutic target in a number of cancers including melanomas, breast cancers, and rhabdomyosarcomas. Described here is the development of a robust and miniaturized biochemical assay for Yes1 kinase that was applied in a high throughput screen (HTS) of kinase-focused small molecule libraries. The HTS provided 144 (17% hit rate) small molecule compounds with IC₅₀ values in the sub-micromolar range. Three of the most potent Yes1 inhibitors were then examined in a cell-based assay for inhibition of cell survival in rhabdomyosarcoma cell lines. Homology models of Yes1 were generated in active and inactive conformations, and docking of inhibitors supports binding to the active conformation (DFG-in) of Yes1. This is the first report of a large high throughput enzymatic activity screen for identification of Yes1 kinase inhibitors, thereby elucidating the polypharmacology of a variety of small molecules and clinical candidates.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Binding Sites
  • Cell Line
  • Cell Survival / drug effects
  • Drug Design
  • Humans
  • Hydrogen Bonding
  • Molecular Docking Simulation
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry*
  • Protein Kinase Inhibitors / toxicity
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins c-yes / antagonists & inhibitors*
  • Proto-Oncogene Proteins c-yes / metabolism
  • Small Molecule Libraries / chemical synthesis
  • Small Molecule Libraries / chemistry*
  • Small Molecule Libraries / toxicity
  • Structure-Activity Relationship

Substances

  • Protein Kinase Inhibitors
  • Small Molecule Libraries
  • Proto-Oncogene Proteins c-yes