Design and synthesis of monocyclic beta-lactams as mechanism-based inhibitors of human cytomegalovirus protease

Bioorg Med Chem Lett. 1998 Feb 17;8(4):365-70. doi: 10.1016/s0960-894x(98)00032-8.

Abstract

Mechanism based inhibitors of HCMV protease have been designed based on the monocyclic beta-lactam nucleus, which have been shown to acylate the viral enzyme in a time dependent manner. SAR in a series of monocyclic beta-lactam N-ureas, has defined the size and relative stereochemistry of the C-3 substituent producing a low micromolar inhibitor 17b with good aqueous stability and selectivity over the mammalian serine proteases.

MeSH terms

  • Drug Stability
  • Humans
  • Isomerism
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / pharmacology
  • Serine Endopeptidases / drug effects*
  • Structure-Activity Relationship
  • Substrate Specificity
  • beta-Lactams / chemical synthesis
  • beta-Lactams / chemistry*
  • beta-Lactams / pharmacology

Substances

  • Protease Inhibitors
  • beta-Lactams
  • Serine Endopeptidases
  • assemblin