| Literature DB >> 30475615 |
Akihide Arima1, Ilva Hanun Harlisa2, Takeshi Yoshida1, Makusu Tsutsui1, Masayoshi Tanaka2, Kazumichi Yokota1, Wataru Tonomura1, Jiro Yasuda3, Masateru Taniguchi1, Takashi Washio1, Mina Okochi2, Tomoji Kawai1.
Abstract
Immunosensing is a bioanalytical technique capable of selective detections of pathogens by utilizing highly specific and strong intermolecular interactions between recognition probes and antigens. Here, we exploited the molecular mechanism in artificial nanopores for selective single-virus identifications. We designed hemagglutinin antibody mimicking oligopeptides with a weak affinity to influenza A virus. By functionalizing the pore wall surface with the synthetic peptides, we rendered specificity to virion-nanopore interactions. The ligand binding thereof was found to perturb translocation dynamics of specific viruses in the nanochannel, which facilitated digital typing of influenza by the resistive pulse bluntness. As amino acid sequence degrees of freedom can potentially offer variety of recognition ability to the molecular probes, this peptide nanopore approach can be used as a versatile immunosensor with single-particle sensitivity that promises wide applications in bioanalysis including bacterial and viral screening to infectious disease diagnosis.Entities:
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Year: 2018 PMID: 30475615 DOI: 10.1021/jacs.8b10854
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419