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10.1002/anie.202107730

http://scihub22266oqcxt.onion/10.1002/anie.202107730
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34328683!8426805!34328683
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suck abstract from ncbi


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pmid34328683      Angew+Chem+Int+Ed+Engl 2021 ; 60 (39): 21211-21215
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  • Discovery and Characterization of Spike N-Terminal Domain-Binding Aptamers for Rapid SARS-CoV-2 Detection #MMPMID34328683
  • Kacherovsky N; Yang LF; Dang HV; Cheng EL; Cardle II; Walls AC; McCallum M; Sellers DL; DiMaio F; Salipante SJ; Corti D; Veesler D; Pun SH
  • Angew Chem Int Ed Engl 2021[Sep]; 60 (39): 21211-21215 PMID34328683show ga
  • The coronavirus disease 2019 (COVID-19) pandemic has devastated families and disrupted healthcare, economies and societies across the globe. Molecular recognition agents that are specific for distinct viral proteins are critical components for rapid diagnostics and targeted therapeutics. In this work, we demonstrate the selection of novel DNA aptamers that bind to the SARS-CoV-2 spike glycoprotein with high specificity and affinity (<80 nM). Through binding assays and high resolution cryo-EM, we demonstrate that SNAP1 (SARS-CoV-2 spike protein N-terminal domain-binding aptamer 1) binds to the S N-terminal domain. We applied SNAP1 in lateral flow assays (LFAs) and ELISAs to detect UV-inactivated SARS-CoV-2 at concentrations as low as 5x10(5) copies mL(-1) . SNAP1 is therefore a promising molecular tool for SARS-CoV-2 diagnostics.
  • |Aptamers, Nucleotide/*chemistry[MESH]
  • |COVID-19/*diagnosis/immunology[MESH]
  • |Enzyme-Linked Immunosorbent Assay[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |SARS-CoV-2/immunology/*isolation & purification[MESH]


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