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?:abstract
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Coronavirus disease 2019 caused by the severe acute respiratory syndrome coronavirus (SARS-CoV-2) has become pandemic SARS-CoV-2 causes influenza-like illnesses, respiratory symptoms, serious lung injuries, pneumonia, multi-organ damage, and mortality The genome of coronaviruses contains approximately six open reading frames (ORFs) ORF 1a/b is translated into protein phosphatases 1a and 1ab, which are processed by SARS-CoV-2\'s main protease (M-pro) M-pro is critical for viral gene expression and replication, making it a key drug target The first 3D structure of M-pro in complex with an inhibitor N3 (PDB ID: 6LU7) was reported This study aimed to screen for N3-like structures via the docking method as potent M-pro inhibitors and drug candidates The M-pro-N3 complex (6LU7) was set up in the RCSB Protein Data Bank N3 was expelled from the structure of M-pro using PyMol 2 3 4 0 Novel ligands from PubChem with structures similar to N3 were screened for docking by Pyrx 8 0 and envisioned by PyMol 2 3 4 0 Our research demonstrated that the binding affinity of CID 6476896 was the highest at -7 8 kcal/mol However, only CIDs 7885280 and 6476893 were possible M-pro inhibitors that interacted with the substrate-binding pocket similarly to N3 and could be drug candidates to target the M-pro of SARS-CoV-2
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Coronavirus disease 2019 caused by the severe acute respiratory syndrome coronavirus (SARS-CoV-2) has become pandemic SARS-CoV-2 causes influenza-like illnesses, respiratory symptoms, serious lung injuries, pneumonia, multi-organ damage, and mortality The genome of coronaviruses contains approximately six open reading frames (ORFs) ORF 1a/b is translated into protein phosphatases 1a and 1ab, which are processed by SARS-CoV-2\'s main protease (Mpro) Mprois critical for viral gene expression and replication, making it a key drug target The first 3D structure of Mpro in complex with an inhibitor N3 (PDB ID: 6LU7) was reported This study aimed to screen for N3-like structures via the docking method as potent Mpro inhibitors and drug candidates The Mpro-N3 complex (6LU7) was set up in the RCSB Protein Data Bank N3 was expelled from the structure of Mprousing PyMol 2 3 4 0 Novel ligands from PubChem with structures similar to N3 were screened for docking by Pyrx 8 0 and envisioned by PyMol 2 3 4 0 Our research demonstrated that the binding affinity of CID 6476896 was the highest at -7 8 kcal/mol However, only CIDs 7885280 and 6476893 were possible Mpro inhibitors that interacted with the substrate-binding pocket similarly to N3 and could be drug candidates to target the Mpro of SARS-CoV-2 © 2020 World Research Association All rights reserved
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