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[Image: see text] The β-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.
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10.1021/acscentsci.0c01309
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document_parses/pdf_json/8fa1d354aca7b53a66ff156940836f433f91911d.json; document_parses/pdf_json/6a7dd40337291ff0767ece0ee226de1c27a930da.json
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document_parses/pmc_json/PMC7755081.xml.json
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De Novo Discovery of High-Affinity Peptide Binders for the SARS-CoV-2 Spike Protein
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