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Updated: Feb 15, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Identification of Individual Bacterial Cells through the Intermolecular Interactions with Peptide-Functionalized
Makusu Tsutsui1, Masayoshi Tanaka2, Takahiro Marui2
1The Institute of Scientific and Industrial Research, Osaka University , 8-1, Mihogaoka, Ibaraki, Osaka 567-0047, Japan.
Abstract:
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.
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