Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.3390/ijms22179124 http://scihub22266oqcxt.onion/10.3390/ijms22179124 34502033!8430524!34502033     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Mol+Sci 2021 ; 22 (17): ä Nephropedia Template TP {{tp|p=34502033|t=2021. Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inhibitor through Molecular Dynamics and Binding Free Energy Simulations |pdf=|usr=}}{{34502033}} gab.com Text Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inhibitor through Molecular Dynamics and Binding Free Energy Simulations JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=34502033 #FOAvip The novel coronavirus disease, caused by severe acute respiratory coronavirus 2 (SARS-CoV-2), rapidly spreading around the world, poses a major threat to the global public health. Herein, we demonstrated the binding mechanism of PF-07321332, alpha-ketoamide, lopinavir, and ritonavir to the coronavirus 3-chymotrypsin-like-protease (3CL(pro)) by means of docking and molecular dynamic (MD) simulations. The analysis of MD trajectories of 3CL(pro) with PF-07321332, alpha-ketoamide, lopinavir, and ritonavir revealed that 3CL(pro)-PF-07321332 and 3CL(pro)-alpha-ketoamide complexes remained stable compared with 3CL(pro)-ritonavir and 3CL(pro)-lopinavir. Investigating the dynamic behavior of ligand-protein interaction, ligands PF-07321332 and alpha-ketoamide showed stronger bonding via making interactions with catalytic dyad residues His41-Cys145 of 3CL(pro). Lopinavir and ritonavir were unable to disrupt the catalytic dyad, as illustrated by increased bond length during the MD simulation. To decipher the ligand binding mode and affinity, ligand interactions with SARS-CoV-2 proteases and binding energy were calculated. The binding energy of the bespoke antiviral PF-07321332 clinical candidate was two times higher than that of alpha-ketoamide and three times than that of lopinavir and ritonavir. Our study elucidated in detail the binding mechanism of the potent PF-07321332 to 3CL(pro) along with the low potency of lopinavir and ritonavir due to weak binding affinity demonstrated by the binding energy data. This study will be helpful for the development and optimization of more specific compounds to combat coronavirus disease. Twit Text FOAVip Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inhibitor through Molecular Dynamics and Binding Free Energy Simulations ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=34502033 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34502033 #FOAvip English Wikipedia <ref>{{Cite pmid|34502033}}</ref> Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inhibitor through Molecular Dynamics and Binding Free Energy Simulations #MMPMID34502033 Ahmad B; Batool M; Ain QU; Kim MS; Choi S Int J Mol Sci 2021[Aug]; 22 (17): ä PMID34502033show ga The novel coronavirus disease, caused by severe acute respiratory coronavirus 2 (SARS-CoV-2), rapidly spreading around the world, poses a major threat to the global public health. Herein, we demonstrated the binding mechanism of PF-07321332, alpha-ketoamide, lopinavir, and ritonavir to the coronavirus 3-chymotrypsin-like-protease (3CL(pro)) by means of docking and molecular dynamic (MD) simulations. The analysis of MD trajectories of 3CL(pro) with PF-07321332, alpha-ketoamide, lopinavir, and ritonavir revealed that 3CL(pro)-PF-07321332 and 3CL(pro)-alpha-ketoamide complexes remained stable compared with 3CL(pro)-ritonavir and 3CL(pro)-lopinavir. Investigating the dynamic behavior of ligand-protein interaction, ligands PF-07321332 and alpha-ketoamide showed stronger bonding via making interactions with catalytic dyad residues His41-Cys145 of 3CL(pro). Lopinavir and ritonavir were unable to disrupt the catalytic dyad, as illustrated by increased bond length during the MD simulation. To decipher the ligand binding mode and affinity, ligand interactions with SARS-CoV-2 proteases and binding energy were calculated. The binding energy of the bespoke antiviral PF-07321332 clinical candidate was two times higher than that of alpha-ketoamide and three times than that of lopinavir and ritonavir. Our study elucidated in detail the binding mechanism of the potent PF-07321332 to 3CL(pro) along with the low potency of lopinavir and ritonavir due to weak binding affinity demonstrated by the binding energy data. This study will be helpful for the development and optimization of more specific compounds to combat coronavirus disease. |*COVID-19 Drug Treatment[MESH] |Antiviral Agents/*pharmacology/therapeutic use[MESH] |Catalytic Domain/drug effects[MESH] |Coronavirus 3C Proteases/*antagonists & inhibitors/metabolism[MESH] |Coronavirus Protease Inhibitors/*pharmacology/therapeutic use[MESH] |Humans[MESH] |Lactams/*pharmacology/therapeutic use[MESH] |Leucine/*pharmacology/therapeutic use[MESH] |Lopinavir/pharmacology[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH] |Nitriles/*pharmacology/therapeutic use[MESH] |Proline/*pharmacology/therapeutic use[MESH] |Ritonavir/pharmacology[MESH]Exploring the Binding Mechanism of PF-07321332 SARS-CoV-2 Protease Inh(epmc).pdf DeepDyve Pubget Overpricing