Discovery of a new binding site on human choline kinase α1: design, synthesis, crystallographic studies, and biological evaluation of asymmetrical bispyridinium derivatives

J Med Chem. 2014 Jan 23;57(2):507-15. doi: 10.1021/jm401665x. Epub 2014 Jan 14.

Abstract

Human choline kinase α (CKα) is a validated drug target for the treatment of cancer. In recent years, a large number of CK inhibitors have been synthesized, and one of them is currently being evaluated in Phase I clinical trials as a treatment for solid tumors. Here we have evaluated a new series of asymmetrical biscationic CK inhibitors by means of enzymatic, crystallographic, and antitumor studies. We demonstrate that one of these structures adopts a completely new binding mode not observed before inducing the aperture of an adjacent binding site. This compound shows antiproliferative and apoptotic effects on cancer cells through activation of caspase-3. Therefore, this study not only provides fruitful insights into the design of more efficient compounds that may target different regions in CKα1 but also explains how these compounds induce apoptosis in cancer cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / chemical synthesis*
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology
  • Apoptosis
  • Binding Sites
  • Caspase 3 / metabolism
  • Cell Proliferation / drug effects
  • Choline Kinase / antagonists & inhibitors*
  • Choline Kinase / chemistry
  • Crystallography, X-Ray
  • Drug Design
  • Drug Screening Assays, Antitumor
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • Molecular Docking Simulation
  • Pyridines / chemical synthesis*
  • Pyridines / chemistry
  • Pyridines / pharmacology

Substances

  • Antineoplastic Agents
  • Pyridines
  • CHKA protein, human
  • Choline Kinase
  • Caspase 3