ArticleNanoscale2017
SDS-assisted protein transport through solid-state nanopores.
Article in Nanoscale, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed.
- Review
- Gated MoSJournal of nanobiotechnology · 2026Article
- Full-length protein classification via cysteine fingerprinting in solid-state nanopores.Nature nanotechnology · 2025Article
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
- Sub-5 nm Silicon Nanopore Sensors: Scalable Fabrication via Self-Limiting Metal-Assisted Chemical Etching.ACS applied materials & interfaces · 2025Article
- A generalized protein identification method for novel and diverse sequencing technologies.NAR genomics and bioinformatics · 2024Article
- Single-Molecule Electrical Profiling of Peptides and Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Nanopore DNA sequencing technologies and their applications towards single-molecule proteomics.Nature chemistry · 2024Review
- Molecular Determinants of Current Blockade Produced by Peptide Transport Through a Nanopore.ACS nanoscience Au · 2024Review
- Solid-State Nanopores for Biomolecular Analysis and Detection.Advances in biochemical engineering/biotechnology · 2024Review
- Protein Sizing with 15 nm Conical Biological Nanopore YaxAB.ACS nano · 2023Article
- Unlocking the Power of Nanopores: Recent Advances in Biosensing Applications and Analog Front-End.Biosensors · 2023Review
- Over 30-Fold Enhancement in DNA Translocation Dynamics through Nanoscale Pores Coated with an Anionic Surfactant.Nano letters · 2023Article
- Nanopore sensors for single molecular protein detection: Research progress based on computer simulations.IET nanobiotechnology · 2023Review
- Single-Molecule Protein Fingerprinting with Photonic Hexagonal Boron Nitride Nanopores.Accounts of materials research · 2023Article
- Distinguishing between Similar Miniproteins with Single-Molecule Nanopore Sensing: A Computational Study.ACS nanoscience Au · 2022Article
- Biological nanopores for single-molecule sensing.iScience · 2022Review
- Cataloguing the proteome: Current developments in single-molecule protein sequencing.Biophysics reviews · 2022Review
- Controlled movement of ssDNA conjugated peptide throughChemical science · 2021Article
- Herding cats: Label-based approaches in protein translocation through nanopore sensors for single-molecule protein sequence analysis.iScience · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Using nanopores for single-molecule sequencing of proteins - similar to nanopore-based sequencing of DNA - faces multiple challenges, including unfolding of the complex tertiary structure of the proteins and enforcing their unidirectional translocation through nanopores. Here, we combine molecular dynamics (MD) simulations with single-molecule experiments to investigate the utility of SDS (Sodium Dodecyl Sulfate) to unfold proteins for solid-state nanopore translocation, while simultaneously endowing them with a stronger electrical charge. Our simulations and experiments prove that SDS-treated proteins show a considerable loss of the protein structure during the nanopore translocation. Moreover, SDS-treated proteins translocate through the nanopore in the direction prescribed by the electrophoretic force due to the negative charge impaired by SDS. In summary, our results suggest that SDS causes protein unfolding while facilitating protein translocation in the direction of the electrophoretic force; both characteristics being advantageous for future protein sequencing applications using solid-state nanopores.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.