ArticleComputational and structural biotechnology journal2021
Spontaneous binding of potential COVID-19 drugs (Camostat and Nafamostat) to human serine protease TMPRSS2.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- In Silico Analysis of CMolecules (Basel, Switzerland) · 2025Article
- Soybean Trypsin Inhibitor Possesses Potency Against SARS-CoV-2 Infection by Blocking the Host Cell Surface Receptors ACE2, TMPRSS2, and CD147.International journal of molecular sciences · 2025Article
- Review
- Identification of potential Indonesian marine invertebrate bioactive compounds as TMPRSS2 and SARS-CoV-2 Omicron spike protein inhibitors through computational screening.Arabian journal of chemistry · 2023Article
- Inhibition of Listeria Monocytogenes HtrA Protease with Camostat, Gabexate and Nafamostat Mesylates and the Binding Mode of the Inhibitors.The protein journal · 2023Article
- Article
- Impact of various buffers and weak bases on lysosomal and intracellular pH: Implications for infectivity of SARS-CoV-2.FASEB bioAdvances · 2023Article
- Extracellular Vesicle-Based SARS-CoV-2 Vaccine.Vaccines · 2023Review
- Highlights on molecular targets in the management of COVID-19: Possible role of pharmacogenomics.The Journal of international medical research · 2023Review
- Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase.Nature communications · 2022Article
- Structural study of the uPA-nafamostat complex reveals a covalent inhibitory mechanism of nafamostat.Biophysical journal · 2022Article
- Targeting SARS-CoV-2 Main Protease for Treatment of COVID-19: Covalent Inhibitors Structure-Activity Relationship Insights and Evolution Perspectives.Journal of medicinal chemistry · 2022Review
- Review
- Molecular dynamics studies reveal structural and functional features of the SARS-CoV-2 spike protein.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Review
- Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants.Signal transduction and targeted therapy · 2022Review
- Camostat Does Not Inhibit the Proteolytic Activity of Neutrophil Serine Proteases.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Pharmacokinetics of Nafamostat, a Potent Serine Protease Inhibitor, by a Novel LC-MS/MS Analysis.Molecules (Basel, Switzerland) · 2022Article
- Discovery of diminazene as a dual inhibitor of SARS-CoV-2 human host proteases TMPRSS2 and furin using cell-based assays.Current research in chemical biology · 2022Article
- Repurposing of thermally stable nucleic-acid aptamers for targeting tetrodotoxin (TTX).Computational and structural biotechnology journal · 2022Article
- Identification of some dietary flavonoids as potential inhibitors of TMPRSS2 through protein-ligand interaction studies and binding free energy calculations.Structural chemistry · 2022Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effective treatment or vaccine is not yet available for combating SARS coronavirus 2 (SARS-CoV-2) that caused the COVID-19 pandemic. Recent studies showed that two drugs, Camostat and Nafamostat, might be repurposed to treat COVID-19 by inhibiting human TMPRSS2 required for proteolytic activation of viral spike (S) glycoprotein. However, their molecular mechanisms of pharmacological action remain unclear. Here, we perform molecular dynamics simulations to investigate their native binding sites on TMPRSS2. We revealed that both drugs could spontaneously and stably bind to the TMPRSS2 catalytic center, and thereby inhibit its proteolytic processing of the S protein. Also, we found that Nafamostat is more specific than Camostat for binding to the catalytic center, consistent with reported observation that Nafamostat blocks the SARS-CoV-2 infection at a lower concentration. Thus, this study provides mechanistic insights into the Camostat and Nafamostat inhibition of the SARS-CoV-2 infection, and offers useful information for COVID-19 drug development.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.