ArticleInternational journal of molecular sciences2023
Stabilization of the Dimeric State of SARS-CoV-2 Main Protease by GC376 and Nirmatrelvir.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Linking biochemical and cellular efficacy of MERS coronavirus main protease inhibitors.ACS pharmacology & translational science · 2026Article
- Linking biochemical and cellular efficacy of MERS coronavirus main protease inhibitors.bioRxiv : the preprint server for biology · 2026Article
- Evaluating the Antifungal Potential of Autophagy-Related Protein 4 (ATG4) Inhibitors against Human Fungal Pathogens.Journal of microbiology and biotechnology · 2025Article
- A SARS-CoV-2 MNature communications · 2025Article
- Article
- Inhibitor-induced dimerization mediates lufotrelvir resistance in mutants of SARS-CoV-2 3C-like protease.Protein science : a publication of the Protein Society · 2025Article
- Enzyme kinetics model for the coronavirus main protease including dimerization and ligand binding.Biophysical journal · 2025Article
- An Investigation of Nirmatrelvir (Paxlovid) Resistance in SARS-CoV-2 MACS bio & med chem Au · 2024Article
- Backstage Heroes-Yeast in COVID-19 Research.International journal of molecular sciences · 2024Review
- Advances in the Search for SARS-CoV-2 MPathogens (Basel, Switzerland) · 2024Review
- High-Resolution Substrate Specificity Profiling of SARS-CoV-2 MACS chemical biology · 2024Article
- A potential allosteric inhibitor of SARS-CoV-2 main protease (MFrontiers in molecular biosciences · 2024Article
- The hope and hype of ellagic acid and urolithins as ligands of SARS-CoV-2 Nsp5 and inhibitors of viral replication.Journal of enzyme inhibition and medicinal chemistry · 2023Article
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Authors and funding
20 authors at 4 institutions in 2 countries.
Funding
Abstract
The main protease (Mpro or 3CLpro) is an enzyme that is evolutionarily conserved among different genera of coronaviruses. As it is essential for processing and maturing viral polyproteins, Mpro has been identified as a promising target for the development of broad-spectrum drugs against coronaviruses. Like SARS-CoV and MERS-CoV, the mature and active form of SARS-CoV-2 Mpro is a dimer composed of identical subunits, each with a single active site. Individual monomers, however, have very low or no catalytic activity. As such, inhibition of Mpro can be achieved by molecules that target the substrate binding pocket to block catalytic activity or target the dimerization process. In this study, we investigated GC376, a transition-state analog inhibitor of the main protease of feline infectious peritonitis coronavirus, and Nirmatrelvir (NMV), an oral, bioavailable SARS-CoV-2 Mpro inhibitor with pan-human coronavirus antiviral activity. Our results show that both GC376 and NMV are capable of strongly binding to SARS-CoV-2 Mpro and altering the monomer-dimer equilibrium by stabilizing the dimeric state. This behavior is proposed to be related to a structured hydrogen-bond network established at the Mpro active site, where hydrogen bonds between Ser1' and Glu166/Phe140 are formed in addition to those achieved by the latter residues with GC376 or NMV.
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Registered trials
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