Molecular modelling studies and in vitro enzymatic assays identified A 4-(nitrobenzyl)guanidine derivative as inhibitor of SARS-CoV-2 Mpro

Sci Rep. 2024 Apr 14;14(1):8620. doi: 10.1038/s41598-024-59292-0.

Abstract

Scientists and researchers have been searching for drugs targeting the main protease (Mpro) of SARS-CoV-2, which is crucial for virus replication. This study employed a virtual screening based on molecular docking to identify benzoylguanidines from an in-house chemical library that can inhibit Mpro on the active site and three allosteric sites. Molecular docking was performed on the LaSMMed Chemical Library using 88 benzoylguanidine compounds. Based on their RMSD values and conserved pose, three potential inhibitors (BZG1, BZG2, and BZG3) were selected. These results indicate that BZG1 and BZG3 may bind to the active site, while BZG2 may bind to allosteric sites. Molecular dynamics data suggest that BZG2 selectively targets allosteric site 3. In vitro tests were performed to measure the proteolytic activity of rMpro. The tests showed that BZG2 has uncompetitive inhibitory activity, with an IC50 value of 77 µM. These findings suggest that benzoylguanidines possess potential as Mpro inhibitors and pave the way towards combating SARS-Cov-2 effectively.

Keywords: 3CL protease; COVID-19; Coronavirus; Inhibitors; Molecular docking; Molecular dynamics.

MeSH terms

  • COVID-19*
  • Enzyme Assays
  • Guanidine
  • Guanidines / pharmacology
  • Humans
  • Molecular Docking Simulation
  • SARS-CoV-2*
  • Small Molecule Libraries

Substances

  • Guanidine
  • Guanidines
  • Small Molecule Libraries