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10.1016/j.bbrc.2020.12.106 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2020.12.106 33454058!7787066!33454058     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Res+Commun 2022 ; 591 (ä): 130-136 Nephropedia Template TP {{tp|p=33454058|t=2022. The inhibitory effects of PGG and EGCG against the SARS-CoV-2 3C-like protease |pdf=|usr=}}{{33454058}} gab.com Text The inhibitory effects of PGG and EGCG against the SARS-CoV-2 3C-like protease JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=33454058 #FOAvip The coronavirus disease (COVID-19) pandemic, resulting from human-to-human transmission of a novel severe acute respiratory syndrome coronavirus (SARS-CoV-2), has led to a global health crisis. Given that the 3 chymotrypsin-like protease (3CLpro) of SARS-CoV-2 plays an indispensable role in viral polyprotein processing, its successful inhibition halts viral replication and thus constrains virus spread. Therefore, developing an effective SARS-CoV-2 3CLpro inhibitor to treat COVID-19 is imperative. A fluorescence resonance energy transfer (FRET)-based method was used to assess the proteolytic activity of SARS-CoV-2 3CLpro using intramolecularly quenched fluorogenic peptide substrates corresponding to the cleavage sequence of SARS-CoV-2 3CLpro. Molecular modeling with GEMDOCK was used to simulate the molecular interactions between drugs and the binding pocket of SARS-CoV-2 3CLpro. This study revealed that the V(max) of SARS-CoV-2 3CLpro was about 2-fold higher than that of SARS-CoV 3CLpro. Interestingly, the proteolytic activity of SARS-CoV-2 3CLpro is slightly more efficient than that of SARS-CoV 3CLpro. Meanwhile, natural compounds PGG and EGCG showed remarkable inhibitory activity against SARS-CoV-2 3CLpro than against SARS-CoV 3CLpro. In molecular docking, PGG and EGCG strongly interacted with the substrate binding pocket of SARS-CoV-2 3CLpro, forming hydrogen bonds with multiple residues, including the catalytic residues C145 and H41. The activities of PGG and EGCG against SARS-CoV-2 3CLpro demonstrate their inhibition of viral protease activity and highlight their therapeutic potentials for treating SARS-CoV-2 infection. Twit Text FOAVip The inhibitory effects of PGG and EGCG against the SARS-CoV-2 3C-like protease ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=33454058 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33454058 #FOAvip English Wikipedia <ref>{{Cite pmid|33454058}}</ref> The inhibitory effects of PGG and EGCG against the SARS-CoV-2 3C-like protease #MMPMID33454058 Chiou WC; Chen JC; Chen YT; Yang JM; Hwang LH; Lyu YS; Yang HY; Huang C Biochem Biophys Res Commun 2022[Feb]; 591 (ä): 130-136 PMID33454058show ga The coronavirus disease (COVID-19) pandemic, resulting from human-to-human transmission of a novel severe acute respiratory syndrome coronavirus (SARS-CoV-2), has led to a global health crisis. Given that the 3 chymotrypsin-like protease (3CLpro) of SARS-CoV-2 plays an indispensable role in viral polyprotein processing, its successful inhibition halts viral replication and thus constrains virus spread. Therefore, developing an effective SARS-CoV-2 3CLpro inhibitor to treat COVID-19 is imperative. A fluorescence resonance energy transfer (FRET)-based method was used to assess the proteolytic activity of SARS-CoV-2 3CLpro using intramolecularly quenched fluorogenic peptide substrates corresponding to the cleavage sequence of SARS-CoV-2 3CLpro. Molecular modeling with GEMDOCK was used to simulate the molecular interactions between drugs and the binding pocket of SARS-CoV-2 3CLpro. This study revealed that the V(max) of SARS-CoV-2 3CLpro was about 2-fold higher than that of SARS-CoV 3CLpro. Interestingly, the proteolytic activity of SARS-CoV-2 3CLpro is slightly more efficient than that of SARS-CoV 3CLpro. Meanwhile, natural compounds PGG and EGCG showed remarkable inhibitory activity against SARS-CoV-2 3CLpro than against SARS-CoV 3CLpro. In molecular docking, PGG and EGCG strongly interacted with the substrate binding pocket of SARS-CoV-2 3CLpro, forming hydrogen bonds with multiple residues, including the catalytic residues C145 and H41. The activities of PGG and EGCG against SARS-CoV-2 3CLpro demonstrate their inhibition of viral protease activity and highlight their therapeutic potentials for treating SARS-CoV-2 infection. |*Molecular Docking Simulation[MESH] |Binding Sites[MESH] |COVID-19/epidemiology/prevention & control/virology[MESH] |Catechin/*analogs & derivatives/chemistry/metabolism/pharmacology[MESH] |Coronavirus 3C Proteases/*antagonists & inhibitors/chemistry/metabolism[MESH] |Drug Evaluation, Preclinical/methods[MESH] |Humans[MESH] |Hydrolyzable Tannins/chemistry/metabolism/*pharmacology[MESH] |Kinetics[MESH] |Models, Molecular[MESH] |Molecular Structure[MESH] |Pandemics[MESH] |Protease Inhibitors/chemistry/metabolism/pharmacology[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |SARS-CoV-2/*drug effects/enzymology/physiology[MESH]The inhibitory effects of PGG and EGCG against the SARS-CoV-2 3C-like (epmc).pdf DeepDyve Pubget Overpricing