Proteasome inhibition by peptide-semicarbazones

Bioorg Med Chem. 2008 Apr 15;16(8):4579-88. doi: 10.1016/j.bmc.2008.02.042. Epub 2008 Feb 15.

Abstract

Peptide-semicarbazones derived from Z-Trp-Trp-Phe-aldehyde inhibit the chymotryptic activity of the human proteasome at nanomolar concentrations, but are less active in a NFkappaB reporter gene assay. Cyclic semicarbazones, in contrast, combine a strong inhibitory effect on the enzyme with an inhibition of NFkappaB signaling in the nanomolar range. In addition, a practical synthesis for scale-up of such compounds was developed.

MeSH terms

  • Cell Proliferation / drug effects
  • Cells, Cultured
  • Humans
  • Immunosuppressive Agents / chemical synthesis
  • Immunosuppressive Agents / chemistry
  • Immunosuppressive Agents / pharmacology
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Structure
  • NF-kappa B / metabolism
  • Peptides / chemistry*
  • Protease Inhibitors / chemical synthesis*
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / pharmacology*
  • Proteasome Endopeptidase Complex / chemistry
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors*
  • Semicarbazones / chemical synthesis*
  • Semicarbazones / chemistry
  • Semicarbazones / pharmacology*
  • Sensitivity and Specificity
  • Signal Transduction / drug effects
  • Structure-Activity Relationship

Substances

  • Immunosuppressive Agents
  • NF-kappa B
  • Peptides
  • Protease Inhibitors
  • Proteasome Inhibitors
  • Semicarbazones
  • Proteasome Endopeptidase Complex