ArticleAdvanced functional materials2016
Graphene Nanopores for Protein Sequencing.
Article in Advanced functional materials, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
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Who cites it
33 citing papers in PubMed, 126 citations in OpenAlex.
- Graphene Nanopore Fabrication and Applications.International journal of molecular sciences · 2025Review
- Graphite-Based Bio-Mimetic Nanopores for Protein Sequencing and Beyond.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Peptide sequencing based on host-guest interaction-assisted nanopore sensing.Nature methods · 2024Article
- Nanopore sensors for single molecular protein detection: Research progress based on computer simulations.IET nanobiotechnology · 2023Review
- Portable nanopore-sequencing technology: Trends in development and applications.Frontiers in microbiology · 2023Review
- Ab Initio Properties of Hybrid Cove-Edged Graphene Nanoribbons as Metallic Electrodes for Peptide Sequencing via Transverse Tunneling Current.ACS omega · 2022Article
- Translocation Behaviors of Synthetic Polyelectrolytes through Alpha-Hemolysin (α-HL) andJournal of the Electrochemical Society · 2022Article
- Zero-mode waveguides and nanopore-based sequencing technologies accelerate single-molecule studies.Biophysics and physicobiology · 2022Article
- Article
- Multiplex quantitative detection of SARS-CoV-2 specific IgG and IgM antibodies based on DNA-assisted nanopore sensing.Biosensors & bioelectronics · 2021Article
- Tuning the binding behaviors of a protein YAP65WW domain on graphenic nano-sheets with boron or nitrogen atom doping.Nanoscale advances · 2020Article
- Enabling nanopore technology for sensing individual amino acids by a derivatization strategy.Journal of materials chemistry. B · 2020Article
- Sensing with Nanopores and Aptamers: A Way Forward.Sensors (Basel, Switzerland) · 2020Review
- N-Terminal Derivatization-Assisted Identification of Individual Amino Acids Using a Biological Nanopore Sensor.ACS sensors · 2020Article
- Application of Solid-State Nanopore in Protein Detection.International journal of molecular sciences · 2020Review
- Insight into the effects of electrochemical factors on host-guest interaction induced signature events in a biological nanopore.Nanotechnology and Precision Engineering · 2020Article
- Electrical recognition of the twenty proteinogenic amino acids using an aerolysin nanopore.Nature biotechnology · 2020Article
- Nanopore Fabrication and Application as Biosensors in Neurodegenerative Diseases.Critical reviews in biomedical engineering · 2020Review
- Beyond mass spectrometry, the next step in proteomics.Science advances · 2020Review
- Biophysics and the Genomic Sciences.Biophysical journal · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
An inexpensive, reliable method for protein sequencing is essential to unraveling the biological mechanisms governing cellular behavior and disease. Current protein sequencing methods suffer from limitations associated with the size of proteins that can be sequenced, the time, and the cost of the sequencing procedures. Here, we report the results of all-atom molecular dynamics simulations that investigated the feasibility of using graphene nanopores for protein sequencing. We focus our study on the biologically significant phenylalanine-glycine repeat peptides (FG-nups)-parts of the nuclear pore transport machinery. Surprisingly, we found FG-nups to behave similarly to single stranded DNA: the peptides adhere to graphene and exhibit step-wise translocation when subject to a transmembrane bias or a hydrostatic pressure gradient. Reducing the peptide's charge density or increasing the peptide's hydrophobicity was found to decrease the translocation speed. Yet, unidirectional and stepwise translocation driven by a transmembrane bias was observed even when the ratio of charged to hydrophobic amino acids was as low as 1:8. The nanopore transport of the peptides was found to produce stepwise modulations of the nanopore ionic current correlated with the type of amino acids present in the nanopore, suggesting that protein sequencing by measuring ionic current blockades may be possible.
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What OpenQuestion holds
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.