ArticleACS nano2022
β-Barrel Nanopores with an Acidic-Aromatic Sensing Region Identify Proteinogenic Peptides at Low pH.
Article in ACS nano, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 52 citations in OpenAlex.
- Sub-Nanomolar Detection and Discrimination of Microcystin Congeners Using Aerolysin Nanopores.ACS nano · 2026Article
- Single-Molecule Fingerprinting of Unlabeled Full-Length Proteins Using an Aerolysin Nanopore.Journal of the American Chemical Society · 2026Article
- Epx4 Nanopore With Multiple Constrictions for Single-Molecule Identification.Small methods · 2026Article
- Machine learning assisted single-molecule sensing towards standard-free quantification of per- and polyfluoroalkyl carboxylic acids.Nature communications · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Comparison among Amber-ff14SB, Amber-ff19SB, and CHARMM36 Force Fields for Ionic and Electroosmotic Flows in Biological Nanopores.Journal of chemical theory and computation · 2025Article
- Protein Design Meets Single-Molecule Detection: Towards Programmable Nanopore Sensors.International journal of molecular sciences · 2025Review
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
- High sensitivity detection of Hepatitis B virus RNA based on 3D-DNA nanomachine and protein nanopore sensing.Molecular biomedicine · 2025Article
- Nanopore discrimination of rare earth elements.Nature nanotechnology · 2025Article
- Redesign of Translocon EXP2 Nanopore for Detecting Peptide Fragments.Small methods · 2025Article
- Nanopore-Functionalized Hybrid Lipid-Block Copolymer Membranes Allow Efficient Single-Molecule Sampling and Stable Sensing of Human Serum.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Toward single-molecule protein sequencing using nanopores.Nature biotechnology · 2025Review
- Direct Identification of O-Glycopeptides by Low-Temperature Assisted Nanopore Technique.Research (Washington, D.C.) · 2025Article
- Controlled Translocation of Proteins through a Biological Nanopore for Single-Protein Fingerprint Identification.Nano letters · 2024Article
- Blobs form during the single-file transport of proteins across nanopores.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Nanopore analysis of cis-diols in fruits.Nature communications · 2024Article
- Programming co-assembled peptide nanofiber morphology via anionic amino acid type: Insights from molecular dynamics simulations.PLoS computational biology · 2023Article
- Review
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological nanopores are emerging as sensitive single-molecule sensors for proteins and peptides. The heterogeneous charge of a polypeptide chain, however, can complicate or prevent the capture and translocation of peptides and unfolded proteins across nanopores. Here, we show that two β-barrel nanopores, aerolysin and cytotoxin K, cannot efficiently detect proteinogenic peptides from a trypsinated protein under a wide range of conditions. However, the introduction of an acidic-aromatic sensing region in the β-barrel dramatically increased the dwell time and the discrimination of peptides in the nanopore at acidic pH. Surprisingly, despite the fact that the two β-barrel nanopores have a similar diameter and an acidic-aromatic construction, their capture mechanisms differ. The electro-osmotic flow played a dominant role for aerolysin, while the electrophoretic force dominated for cytotoxin K. Nonetheless, both β-barrel nanopores allowed the detection of mixtures of trypsinated peptides, with aerolysin nanopores showing a better resolution for larger peptides and cytotoxin K showing a better resolution for shorter peptides. Therefore, this work provides a generic strategy for modifying nanopores for peptide detection that will be most likely be applicable to other nanopore-forming toxins.
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