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10.1021/acsnano.0c04798 http://scihub22266oqcxt.onion/10.1021/acsnano.0c04798 32806067!ä!32806067 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Nano 2020 ; 14 (8): 10616-10623 Nephropedia Template TP {{tp|p=32806067|t=2020. Enhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Polybasic Cleavage Sites |pdf=|usr=}}{{32806067}} gab.com Text Enhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Polybasic Cleavage Sites JO: ACS Nano http://www.kidney.de/pget.php?&tw=1&pmid=32806067 #FOAvip The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein plays a crucial role in binding the human cell receptor ACE2 that is required for viral entry. Many studies have been conducted to target the structures of RBD-ACE2 binding and to design RBD-targeting vaccines and drugs. Nevertheless, mutations distal from the SARS-CoV-2 RBD also impact its transmissibility and antibody can target non-RBD regions, suggesting the incomplete role of the RBD region in the spike protein-ACE2 binding. Here, in order to elucidate distant binding mechanisms, we analyze complexes of ACE2 with the wild-type spike protein and with key mutants via large-scale all-atom explicit solvent molecular dynamics simulations. We find that though distributed approximately 10 nm away from the RBD, the SARS-CoV-2 polybasic cleavage sites enhance, via electrostatic interactions and hydration, the RBD-ACE2 binding affinity. A negatively charged tetrapeptide (GluGluLeuGlu) is then designed to neutralize the positively charged arginine on the polybasic cleavage sites. We find that the tetrapeptide GluGluLeuGlu binds to one of the three polybasic cleavage sites of the SARS-CoV-2 spike protein lessening by 34% the RBD-ACE2 binding strength. This significant binding energy reduction demonstrates the feasibility to neutralize RBD-ACE2 binding by targeting this specific polybasic cleavage site. Our work enhances understanding of the binding mechanism of SARS-CoV-2 to ACE2, which may aid the design of therapeutics for COVID-19 infection. Twit Text FOAVip Enhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Polybasic Cleavage Sites ????ACS Nano http://www.kidney.de/pget.php?&tw=1&pmid=32806067 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32806067 #FOAvip English Wikipedia <ref>{{Cite pmid|32806067}}</ref> Enhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Polybasic Cleavage Sites #MMPMID32806067 Qiao B; Olvera de la Cruz M ACS Nano 2020[Aug]; 14 (8): 10616-10623 PMID32806067show ga The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein plays a crucial role in binding the human cell receptor ACE2 that is required for viral entry. Many studies have been conducted to target the structures of RBD-ACE2 binding and to design RBD-targeting vaccines and drugs. Nevertheless, mutations distal from the SARS-CoV-2 RBD also impact its transmissibility and antibody can target non-RBD regions, suggesting the incomplete role of the RBD region in the spike protein-ACE2 binding. Here, in order to elucidate distant binding mechanisms, we analyze complexes of ACE2 with the wild-type spike protein and with key mutants via large-scale all-atom explicit solvent molecular dynamics simulations. We find that though distributed approximately 10 nm away from the RBD, the SARS-CoV-2 polybasic cleavage sites enhance, via electrostatic interactions and hydration, the RBD-ACE2 binding affinity. A negatively charged tetrapeptide (GluGluLeuGlu) is then designed to neutralize the positively charged arginine on the polybasic cleavage sites. We find that the tetrapeptide GluGluLeuGlu binds to one of the three polybasic cleavage sites of the SARS-CoV-2 spike protein lessening by 34% the RBD-ACE2 binding strength. This significant binding energy reduction demonstrates the feasibility to neutralize RBD-ACE2 binding by targeting this specific polybasic cleavage site. Our work enhances understanding of the binding mechanism of SARS-CoV-2 to ACE2, which may aid the design of therapeutics for COVID-19 infection. |Amino Acid Substitution[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Antiviral Agents/chemistry/pharmacology[MESH] |Betacoronavirus/chemistry/genetics/*metabolism[MESH] |Binding Sites/genetics[MESH] |COVID-19[MESH] |Coronavirus Infections/*virology[MESH] |Drug Design[MESH] |Host Microbial Interactions/drug effects[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Mutation[MESH] |Oligopeptides/chemistry/pharmacology[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/chemistry/genetics/*metabolism[MESH] |Pneumonia, Viral/*virology[MESH] |Protein Binding/drug effects/genetics/physiology[MESH] |Protein Domains[MESH] |Receptors, Virus/chemistry/genetics/*metabolism[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/chemistry/genetics/*metabolism[MESH]Enhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Pol(epmc).pdf DeepDyve Pubget Overpricing