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10.1080/07391102.2021.1889665 http://scihub22266oqcxt.onion/10.1080/07391102.2021.1889665 33645443!7938657!33645443     free     free     free 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       J+Biomol+Struct+Dyn 2022 ; 40 (14): 6671-6681 Nephropedia Template TP {{tp|p=33645443|t=2022. A potential peptide inhibitor of SARS-CoV-2 S and human ACE2 complex |pdf=|usr=}}{{33645443}} gab.com Text A potential peptide inhibitor of SARS-CoV-2 S and human ACE2 complex JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=33645443 #FOAvip The disease COVID-19 has caused heavy socio-economic burden and there is immediate need to control it. The disease is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus. The viral entry into human cell depends on the attachment of spike (S) protein via its receptor binding domain (RBD) to human cell receptor angiotensin-converting enzyme 2 (hACE2). Thus, blocking the virus attachment to hACE2 could serve as potential therapeutics for viral infection. We have designed a peptide inhibitor (DeltaABP-alpha2) targeting the RBD of S protein using in-silico approach. Docking studies and computed affinities suggested that peptide inhibitor binds at the RBD with approximately 95-fold higher affinity than hACE2. Molecular dynamics (MD) simulation confirms the stable binding of inhibitor to hACE2. Immunoinformatics studies suggest non-immunogenic and non-toxic nature of peptide. Thus, the proposed peptide could serve as potential blocker for viral attachment.Communicated by Ramaswamy H. Sarma. Twit Text FOAVip A potential peptide inhibitor of SARS-CoV-2 S and human ACE2 complex ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=33645443 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33645443 #FOAvip English Wikipedia <ref>{{Cite pmid|33645443}}</ref> A potential peptide inhibitor of SARS-CoV-2 S and human ACE2 complex #MMPMID33645443 Jaiswal G; Yaduvanshi S; Kumar V J Biomol Struct Dyn 2022[Sep]; 40 (14): 6671-6681 PMID33645443show ga The disease COVID-19 has caused heavy socio-economic burden and there is immediate need to control it. The disease is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus. The viral entry into human cell depends on the attachment of spike (S) protein via its receptor binding domain (RBD) to human cell receptor angiotensin-converting enzyme 2 (hACE2). Thus, blocking the virus attachment to hACE2 could serve as potential therapeutics for viral infection. We have designed a peptide inhibitor (DeltaABP-alpha2) targeting the RBD of S protein using in-silico approach. Docking studies and computed affinities suggested that peptide inhibitor binds at the RBD with approximately 95-fold higher affinity than hACE2. Molecular dynamics (MD) simulation confirms the stable binding of inhibitor to hACE2. Immunoinformatics studies suggest non-immunogenic and non-toxic nature of peptide. Thus, the proposed peptide could serve as potential blocker for viral attachment.Communicated by Ramaswamy H. Sarma. |*Angiotensin-Converting Enzyme 2[MESH] |*COVID-19 Drug Treatment[MESH] |Binding Sites[MESH] |Humans[MESH] |Peptides/metabolism/pharmacology[MESH] |Peptidyl-Dipeptidase A/chemistry[MESH] |Protein Binding[MESH] |SARS-CoV-2[MESH]A potential peptide inhibitor of SARS-CoV-2 S and human ACE2 complex (epmc).pdf DeepDyve Pubget Overpricing