Structure-based design, synthesis, and biological evaluation of peptidomimetic SARS-CoV 3CLpro inhibitors

Bioorg Med Chem Lett. 2007 Nov 1;17(21):5876-80. doi: 10.1016/j.bmcl.2007.08.031. Epub 2007 Aug 19.

Abstract

Structure-based design, synthesis, and biological evaluation of a series of peptidomimetic severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors are described. These inhibitors were designed and synthesized based upon our X-ray crystal structure of inhibitor 1 bound to SARS-CoV 3CLpro. Incorporation of Boc-Ser as the P(4)-ligand resulted in enhanced SARS-CoV 3CLpro inhibitory activity. Structural analysis of the inhibitor-bound X-ray structure revealed high binding affinity toward the enzyme.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Coronavirus 3C Proteases
  • Crystallography, X-Ray
  • Cysteine Endopeptidases
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Mimicry*
  • Molecular Structure
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / pharmacology*
  • Viral Proteins / antagonists & inhibitors*

Substances

  • Protease Inhibitors
  • Viral Proteins
  • Cysteine Endopeptidases
  • Coronavirus 3C Proteases