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10.1016/j.ijantimicag.2020.106119

http://scihub22266oqcxt.onion/10.1016/j.ijantimicag.2020.106119
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32738306!7390782!32738306
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suck abstract from ncbi


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pmid32738306      Int+J+Antimicrob+Agents 2020 ; 56 (3): 106119
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  • In silico study of azithromycin, chloroquine and hydroxychloroquine and their potential mechanisms of action against SARS-CoV-2 infection #MMPMID32738306
  • Braz HLB; Silveira JAM; Marinho AD; de Moraes MEA; Moraes Filho MO; Monteiro HSA; Jorge RJB
  • Int J Antimicrob Agents 2020[Sep]; 56 (3): 106119 PMID32738306show ga
  • Coronavirus disease 2019 (COVID-19) is a highly transmissible viral infection caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Clinical trials have reported improved outcomes resulting from an effective reduction or absence of viral load when patients were treated with chloroquine (CQ) or hydroxychloroquine (HCQ). In addition, the effects of these drugs were improved by simultaneous administration of azithromycin (AZM). The receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein binds to the cell surface angiotensin-converting enzyme 2 (ACE2) receptor, allowing virus entry and replication in host cells. The viral main protease (M(pro)) and host cathepsin L (CTSL) are among the proteolytic systems involved in SARS-CoV-2 S protein activation. Hence, molecular docking studies were performed to test the binding performance of these three drugs against four targets. The findings showed AZM affinity scores (DeltaG) with strong interactions with ACE2, CTSL, M(pro) and RBD. CQ affinity scores showed three low-energy results (less negative) with ACE2, CTSL and RBD, and a firm bond score with M(pro). For HCQ, two results (ACE2 and M(pro)) were firmly bound to the receptors, however CTSL and RBD showed low interaction energies. The differences in better interactions and affinity between HCQ and CQ with ACE2 and M(pro) were probably due to structural differences between the drugs. On other hand, AZM not only showed more negative (better) values in affinity, but also in the number of interactions in all targets. Nevertheless, further studies are needed to investigate the antiviral properties of these drugs against SARS-CoV-2.
  • |Amino Acid Motifs[MESH]
  • |Angiotensin-Converting Enzyme 2[MESH]
  • |Antiviral Agents/chemistry/*pharmacology[MESH]
  • |Azithromycin/*chemistry/pharmacology[MESH]
  • |Betacoronavirus/*chemistry/metabolism[MESH]
  • |Binding Sites[MESH]
  • |COVID-19[MESH]
  • |Cathepsin L/antagonists & inhibitors/*chemistry/metabolism[MESH]
  • |Chloroquine/*chemistry/pharmacology[MESH]
  • |Coronavirus 3C Proteases[MESH]
  • |Coronavirus Infections/drug therapy/virology[MESH]
  • |Cysteine Endopeptidases/*chemistry/metabolism[MESH]
  • |Host-Pathogen Interactions/drug effects/genetics[MESH]
  • |Humans[MESH]
  • |Hydroxychloroquine/*chemistry/pharmacology[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Pandemics[MESH]
  • |Peptidyl-Dipeptidase A/*chemistry/genetics/metabolism[MESH]
  • |Pneumonia, Viral/drug therapy/virology[MESH]
  • |Protein Binding[MESH]
  • |Protein Interaction Domains and Motifs[MESH]
  • |Protein Structure, Secondary[MESH]
  • |SARS-CoV-2[MESH]
  • |Spike Glycoprotein, Coronavirus/antagonists & inhibitors/*chemistry/genetics/metabolism[MESH]
  • |Thermodynamics[MESH]
  • |Viral Nonstructural Proteins/antagonists & inhibitors/*chemistry/metabolism[MESH]


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