Sugar amino acid based peptide epoxyketones as potential proteasome inhibitors

Bioorg Chem. 2010 Oct;38(5):202-9. doi: 10.1016/j.bioorg.2010.04.004. Epub 2010 Apr 28.

Abstract

This paper describes the synthesis and biological evaluation of nine epoxomicin-derived sugar amino acid containing peptide epoxyketones. The title compounds are assembled from six sugar amino acid dipeptide isosteres and are synthesized using solution-phase peptide synthesis protocols. Although neither of the compounds displays inhibitory activity towards any of the proteasome active sites, our approach holds promise towards the development of structurally new proteasome inhibitors. It is likely that the central sugar amino acid dipeptide isoster needs to be designed such that it closely resemble dipeptides at position P2 and P3 in proteasome substrates inhibitors, such as the Thr-Ile dipeptide present in the lead compound, epoxomicin.

MeSH terms

  • Amino Acids / chemical synthesis
  • Amino Acids / chemistry
  • Amino Acids / pharmacology
  • Cell Line
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Ketones / chemical synthesis
  • Ketones / chemistry
  • Ketones / pharmacology
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / pharmacology*
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteasome Inhibitors*
  • Sugar Acids / chemical synthesis
  • Sugar Acids / chemistry
  • Sugar Acids / pharmacology

Substances

  • Amino Acids
  • Enzyme Inhibitors
  • Ketones
  • Oligopeptides
  • Proteasome Inhibitors
  • Sugar Acids
  • Proteasome Endopeptidase Complex
  • epoxomicin