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  • Identification of key interactions between SARS-CoV-2 main protease and inhibitor drug candidates #MMPMID32719454
  • Yoshino R; Yasuo N; Sekijima M
  • Sci Rep 2020[Jul]; 10 (1): 12493 PMID32719454show ga
  • The number of cases of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection (COVID-19) has reached over 114,000. SARS-CoV-2 caused a pandemic in Wuhan, China, in December 2019 and is rapidly spreading globally. It has been reported that peptide-like anti-HIV-1 drugs are effective against SARS-CoV Main protease (M(pro)). Due to the close phylogenetic relationship between SARS-CoV and SARS-CoV-2, their main proteases share many structural and functional features. Thus, these drugs are also regarded as potential drug candidates targeting SARS-CoV-2 M(pro). However, the mechanism of action of SARS-CoV-2 M(pro) at the atomic-level is unknown. In the present study, we revealed key interactions between SARS-CoV-2 M(pro) and three drug candidates by performing pharmacophore modeling and 1 mus molecular dynamics (MD) simulations. His41, Gly143, and Glu166 formed interactions with the functional groups that were common among peptide-like inhibitors in all MD simulations. These interactions are important targets for potential drugs against SARS-CoV-2 M(pro).
  • |Amino Acid Sequence[MESH]
  • |Betacoronavirus/chemistry/isolation & purification/*metabolism[MESH]
  • |Binding Sites[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/pathology/virology[MESH]
  • |Drug Design[MESH]
  • |Humans[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/pathology/virology[MESH]
  • |Protease Inhibitors/*chemistry/metabolism[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |SARS Virus/chemistry/isolation & purification/metabolism[MESH]
  • |SARS-CoV-2[MESH]
  • |Sequence Alignment[MESH]
  • |Viral Nonstructural Proteins/*antagonists & inhibitors/metabolism[MESH]

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  • suck abstract from ncbi

    12493 1.10 2020