Discovery of a potent and highly β1 specific proteasome inhibitor from a focused library of urea-containing peptide vinyl sulfones and peptide epoxyketones

Org Biomol Chem. 2012 Jan 7;10(1):181-94. doi: 10.1039/c1ob06554h. Epub 2011 Nov 22.

Abstract

Syringolins, a class of natural products, potently and selectively inhibit the proteasome and show promising antitumour activity. To gain insight in the mode of action of syringolins, the ureido structural element present in syringolins is incorporated in oligopeptide vinyl sulfones and peptide epoxyketones yielding a focused library of potent new proteasome inhibitors. The distance of the ureido linkage with respect to the electrophilic trap strongly influences subunit selectivity within the proteasome. Compounds 13 and 15 are β5 selective and their potency exceeds that of syringolin A. In contrast, 5 may well be the most potent β1 selective compound active in living cells reported to date.

Publication types

  • Research Support, American Recovery and Reinvestment Act
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Humans
  • Ketones / chemistry
  • Ketones / pharmacology*
  • Peptides / chemistry*
  • Proteasome Inhibitors*
  • Sulfones / chemistry
  • Sulfones / pharmacology*
  • Urea / chemistry*

Substances

  • Ketones
  • Peptides
  • Proteasome Inhibitors
  • Sulfones
  • Urea