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10.2144/btn-2020-0038

http://scihub22266oqcxt.onion/10.2144/btn-2020-0038
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32459144!7273901!32459144
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suck abstract from ncbi


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pmid32459144      Biotechniques 2020 ; 69 (2): 108-112
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  • Discovery of alliin as a putative inhibitor of the main protease of SARS-CoV-2 by molecular docking #MMPMID32459144
  • Cheng B; Li T
  • Biotechniques 2020[Aug]; 69 (2): 108-112 PMID32459144show ga
  • The outbreak of viral pneumonia caused by the novel coronavirus SARS-CoV-2 that began in December 2019 caused high mortality. It has been suggested that the main protease (Mpro) of SARS-CoV-2 may be an important target to discover pharmaceutical compounds for the therapy of this life-threatening disease. Remdesivir, ritonavir and chloroquine have all been reported to play a role in suppressing SARS-CoV-2. Here, we applied a molecular docking method to study the binding stability of these drugs with SARS-CoV-2 Mpro. It appeared that the ligand-protein binding stability of the alliin and SARS-CoV-2 Mpro complex was better than others. The results suggested that alliin may serve as a good candidate as an inhibitor of SARS-CoV-2 Mpro. Therefore, the present research may provide some meaningful guidance for the prevention and treatment of SARS-CoV-2.
  • |Adenosine Monophosphate/analogs & derivatives/pharmacology[MESH]
  • |Alanine/analogs & derivatives/pharmacology[MESH]
  • |Antimalarials/pharmacology[MESH]
  • |Antiviral Agents/*pharmacology[MESH]
  • |Betacoronavirus/enzymology[MESH]
  • |Chloroquine/pharmacology[MESH]
  • |Coronavirus 3C Proteases[MESH]
  • |Cysteine Endopeptidases[MESH]
  • |Cysteine/*analogs & derivatives/pharmacology[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Ritonavir/pharmacology[MESH]
  • |SARS-CoV-2[MESH]


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