Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease

Science. 2020 Jun 19;368(6497):1331-1335. doi: 10.1126/science.abb4489. Epub 2020 Apr 22.

Abstract

SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) is the etiological agent responsible for the global COVID-19 (coronavirus disease 2019) outbreak. The main protease of SARS-CoV-2, Mpro, is a key enzyme that plays a pivotal role in mediating viral replication and transcription. We designed and synthesized two lead compounds (11a and 11b) targeting Mpro Both exhibited excellent inhibitory activity and potent anti-SARS-CoV-2 infection activity. The x-ray crystal structures of SARS-CoV-2 Mpro in complex with 11a or 11b, both determined at a resolution of 1.5 angstroms, showed that the aldehyde groups of 11a and 11b are covalently bound to cysteine 145 of Mpro Both compounds showed good pharmacokinetic properties in vivo, and 11a also exhibited low toxicity, which suggests that these compounds are promising drug candidates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antiviral Agents / chemistry*
  • Antiviral Agents / pharmacology
  • Betacoronavirus / drug effects
  • Betacoronavirus / enzymology*
  • COVID-19
  • Catalytic Domain
  • Chlorocebus aethiops
  • Coronavirus 3C Proteases
  • Coronavirus Infections / drug therapy
  • Cysteine Endopeptidases
  • Dogs
  • Drug Design*
  • Drug Evaluation, Preclinical
  • Female
  • Humans
  • Male
  • Mice
  • Molecular Structure
  • Pandemics
  • Pneumonia, Viral / drug therapy
  • Protein Structure, Tertiary
  • Rats, Sprague-Dawley
  • SARS-CoV-2
  • Toxicity Tests
  • Vero Cells
  • Viral Nonstructural Proteins / antagonists & inhibitors*

Substances

  • Antiviral Agents
  • Viral Nonstructural Proteins
  • Cysteine Endopeptidases
  • Coronavirus 3C Proteases