New, potent P1/P2-morpholinone-based HIV-protease inhibitors

Bioorg Med Chem Lett. 2006 Oct 1;16(19):5226-30. doi: 10.1016/j.bmcl.2006.07.014. Epub 2006 Aug 10.

Abstract

We have developed efficient synthesis of morpholinone-based cyclic mimetics of the P1/P2 portion of the HIV-1 protease inhibitor Amprenavir. This effort led to discovery of allyl- and spiro-cyclopropyl-P2-substituted inhibitors 17 and 31, both 500 times more potent than the parent inhibitor 1. These results support morpholinones as novel mimetics of the P1/P2 portion of Amprenavir and potentially of other HIV-protease inhibitors, and thus provide a novel medicinal chemistry template for optimization toward more potent and drug-like inhibitors.

MeSH terms

  • Carbamates
  • Furans
  • HIV Protease Inhibitors / chemical synthesis*
  • HIV Protease Inhibitors / pharmacology
  • Humans
  • Molecular Mimicry
  • Morpholines / chemical synthesis*
  • Morpholines / pharmacology
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / pharmacology
  • Structure-Activity Relationship
  • Sulfonamides

Substances

  • Carbamates
  • Furans
  • HIV Protease Inhibitors
  • Morpholines
  • Peptides, Cyclic
  • Sulfonamides
  • amprenavir