Selective bisubstrate inhibitors with sub-nanomolar affinity for protein kinase Pim-1

ChemMedChem. 2013 Jun;8(6):909-13. doi: 10.1002/cmdc.201300042. Epub 2013 Apr 24.


Potent and selective: The unique nature of the ATP binding pocket structure of Pim family protein kinases (PKs) was used for the development of bisubstrate inhibitors and a fluorescent probe with sub-nanomolar affinity. Conjugates of arginine-rich peptides with two ATP mimetic scaffolds were synthesized and tested as inhibitors of Pim-1. Against a panel of 124 protein kinases, a novel ARC-PIM conjugate selectively inhibited PKs of the Pim family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dose-Response Relationship, Drug
  • Molecular Structure
  • Nanostructures / chemistry*
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / pharmacology*
  • Proto-Oncogene Proteins c-pim-1 / antagonists & inhibitors*
  • Proto-Oncogene Proteins c-pim-1 / metabolism
  • Structure-Activity Relationship


  • Protein Kinase Inhibitors
  • Proto-Oncogene Proteins c-pim-1