ArticleACS sensors2021
Tuning Protein Discrimination Through Altering the Sampling Interface Formed between the Analyte and the OmpG Nanopore.
Article in ACS sensors, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Review
- Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Simulation of pH-Dependent, Loop-Based Membrane Protein Gating Using Pretzel.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Engineering Linker-Enhanced OmpG Nanopores for Rapid Single-Molecule Protease Detection.Sensors (Basel, Switzerland) · 2025Article
- Protein Design Meets Single-Molecule Detection: Towards Programmable Nanopore Sensors.International journal of molecular sciences · 2025Review
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Sculpting conducting nanopore size and shape through de novo protein design.Science (New York, N.Y.) · 2024Article
- Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023Article
- Confirming Silent Translocation through Nanopores with Simultaneous Single-Molecule Fluorescence and Single-Channel Electrical Recordings.Analytical chemistry · 2023Article
- An Engineered OmpG Nanopore with Displayed Peptide Motifs for Single-Molecule Multiplex Protein Detection.Angewandte Chemie (International ed. in English) · 2023Article
- Modifying the pH sensitivity of OmpG nanopore for improved detection at acidic pH.Biophysical journal · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Nanopore sensors capable of distinguishing homologous protein analytes are highly desirable tools for proteomics research and disease diagnostics. Recently, an engineered outer membrane protein G (OmpG) nanopore with a high-affinity ligand attached to a gating loop 6 showed specificity for distinguishing homologous proteins in complex mixtures. Here, we report the development of OmpG nanopores with the other six loops used as the anchoring point to host an affinity ligand for protein sensing. We investigated how the analyte binding to the affinity ligand located at different loops affects the detection sensitivity, selectivity, and specificity. Our results reveal that analytes weakly attracted to the OmpG nanopore surface are only detectable when the ligand is tethered to loop 6. In contrast, protein analytes that form a strong interaction with the OmpG surface via electrostatic attractions are distinguishable by all seven OmpG nanopore constructs. In addition, the same analyte can generate distinct binding signals with different OmpG nanopore constructs. The ability to exploit all seven OmpG loops will aid the design of a new generation of OmpG sensors with increased sensitivity, selectivity, and specificity for biomarker sensing.
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