Jump to Main Content
Identification of Individual Bacterial Cells through the Intermolecular Interactions with Peptide-Functionalized Solid-State Pores
- Tsutsui, Makusu, Tanaka, Masayoshi, Marui, Takahiro, Yokota, Kazumichi, Yoshida, Takeshi, Arima, Akihide, Tonomura, Wataru, Taniguchi, Masateru, Washio, Takashi, Okochi, Mina, Kawai, Tomoji
- Analytical chemistry 2018 v.90 no.3 pp. 1511-1515
- Escherichia coli, Toll-like receptor 5, bacteria, chemical interactions, flagellum, gold, mutants, synthetic peptides
- Bioinspired pore sensing for selective detection of flagellated bacteria was investigated. The Au micropore wall surface was modified with a synthetic peptide designed from toll-like receptor 5 (TLR5) to mimic the pathogen-recognition capability. We found that intermolecular interactions between the TLR5-derived recognition peptides and flagella induce ligand-specific perturbations in the translocation dynamics of Escherichia coli, which facilitated the discrimination between the wild-type and flagellin-deletion mutant (ΔfliC) by the resistive pulse patterns thereby demonstrating the sensing of bacteria at a single-cell level. These results provide a novel concept of utilizing weak intermolecular interactions as a recognition probes for single-cell microbial identification.