Molecular modeling studies toward the structural optimization of new cyclopeptide-based HDAC inhibitors modeled on the natural product FR235222

Bioorg Med Chem. 2008 Sep 15;16(18):8635-42. doi: 10.1016/j.bmc.2008.08.003. Epub 2008 Aug 6.

Abstract

The natural cyclopeptide FR235222 is a potent HDAC inhibitor displaying relevant multiple anticancer effects and is considered an attractive lead compound for the generation of new and more effective antitumor therapeutics. Recently, we have synthesized a small collection of FR235222 simplified analogues which showed interesting biological activities. These results encouraged us to further explore the structural determinants responsible for the activity of this class of HDAC inhibitors in order to gain guidelines for the rational design of new derivatives with putative higher affinity for this target. In the present paper, we report the results obtained, docking these ligands in the binding pocket of HDLP, an HDAC homologue.

MeSH terms

  • Algorithms
  • Antineoplastic Agents / chemical synthesis
  • Antineoplastic Agents / pharmacology*
  • Binding Sites
  • Biological Products / chemical synthesis
  • Biological Products / pharmacology*
  • Computer Simulation
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / pharmacology*
  • Histone Deacetylase Inhibitors*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / pharmacology*
  • Structure-Activity Relationship

Substances

  • Antineoplastic Agents
  • Biological Products
  • Enzyme Inhibitors
  • FR 235222
  • Histone Deacetylase Inhibitors
  • Peptides, Cyclic