Design and synthesis of peptidomimetic severe acute respiratory syndrome chymotrypsin-like protease inhibitors

J Med Chem. 2005 Nov 3;48(22):6767-71. doi: 10.1021/jm050548m.

Abstract

Design, synthesis, and biological evaluation of peptidomimetic severe acute respiratory syndrome chymotrypsin-like protease (SARS-3CLpro) inhibitors for severe acute respiratory syndrome coronavirus (SARS-CoV) are described. These inhibitors exhibited antiviral activity against SARS-CoV in infected cells in the micromolar range. An X-ray crystal structure of our lead inhibitor (4) bound to SARS-3CLpro provided important drug-design templates for the design of small-molecule inhibitors.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antiviral Agents / chemical synthesis*
  • Antiviral Agents / chemistry
  • Antiviral Agents / pharmacology
  • Cells, Cultured
  • Chymases
  • Crystallography, X-Ray
  • Dipeptides / chemistry
  • Drug Design
  • Humans
  • Isoxazoles / chemical synthesis
  • Isoxazoles / chemistry
  • Isoxazoles / pharmacology
  • Kinetics
  • Lactams / chemical synthesis
  • Lactams / chemistry
  • Lactams / pharmacology
  • Models, Molecular
  • Molecular Mimicry
  • Peptides / chemistry*
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / chemical synthesis*
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / pharmacology
  • Severe acute respiratory syndrome-related coronavirus / drug effects
  • Severe acute respiratory syndrome-related coronavirus / enzymology*
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Antiviral Agents
  • Dipeptides
  • Isoxazoles
  • Lactams
  • Peptides
  • Serine Proteinase Inhibitors
  • Serine Endopeptidases
  • Chymases