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10.1021/acscentsci.0c01309 http://scihub22266oqcxt.onion/10.1021/acscentsci.0c01309 33527085!7755081!33527085     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Cent+Sci 2021 ; 7 (1): 156-163 Nephropedia Template TP {{tp|p=33527085|t=2021. De Novo Discovery of High-Affinity Peptide Binders for the SARS-CoV-2 Spike Protein |pdf=|usr=}}{{33527085}} gab.com Text De Novo Discovery of High-Affinity Peptide Binders for the SARS-CoV-2 Spike Protein JO: ACS Cent Sci http://www.kidney.de/pget.php?&tw=1&pmid=33527085 #FOAvip The beta-coronavirus SARS-CoV-2 has caused a global pandemic. Affinity reagents targeting the SARS-CoV-2 spike protein are of interest for the development of therapeutics and diagnostics. We used affinity selection-mass spectrometry for the rapid discovery of synthetic high-affinity peptide binders for the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. From library screening with 800 million synthetic peptides, we identified three sequences with nanomolar affinities (dissociation constants K (d) = 80-970 nM) for RBD and selectivity over human serum proteins. Nanomolar RBD concentrations in a biological matrix could be detected using the biotinylated lead peptide in ELISA format. These peptides do not compete for ACE2 binding, and their site of interaction on the SARS-CoV-2-spike-RBD might be unrelated to the ACE2 binding site, making them potential orthogonal reagents for sandwich immunoassays. These findings serve as a starting point for the development of SARS-CoV-2 diagnostics or conjugates for virus-directed delivery of therapeutics. Twit Text FOAVip De Novo Discovery of High-Affinity Peptide Binders for the SARS-CoV-2 Spike Protein ????ACS Cent Sci http://www.kidney.de/pget.php?&tw=1&pmid=33527085 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33527085 #FOAvip English Wikipedia <ref>{{Cite pmid|33527085}}</ref> De Novo Discovery of High-Affinity Peptide Binders for the SARS-CoV-2 Spike Protein #MMPMID33527085 Pomplun S; Jbara M; Quartararo AJ; Zhang G; Brown JS; Lee YC; Ye X; Hanna S; Pentelute BL ACS Cent Sci 2021[Jan]; 7 (1): 156-163 PMID33527085show ga The beta-coronavirus SARS-CoV-2 has caused a global pandemic. Affinity reagents targeting the SARS-CoV-2 spike protein are of interest for the development of therapeutics and diagnostics. We used affinity selection-mass spectrometry for the rapid discovery of synthetic high-affinity peptide binders for the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. From library screening with 800 million synthetic peptides, we identified three sequences with nanomolar affinities (dissociation constants K (d) = 80-970 nM) for RBD and selectivity over human serum proteins. Nanomolar RBD concentrations in a biological matrix could be detected using the biotinylated lead peptide in ELISA format. These peptides do not compete for ACE2 binding, and their site of interaction on the SARS-CoV-2-spike-RBD might be unrelated to the ACE2 binding site, making them potential orthogonal reagents for sandwich immunoassays. These findings serve as a starting point for the development of SARS-CoV-2 diagnostics or conjugates for virus-directed delivery of therapeutics. äDe Novo Discovery of High-Affinity Peptide Binders for the SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing