ArticleACS nano2019
Interactions of a Polypeptide with a Protein Nanopore Under Crowding Conditions.
Article in ACS nano, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 48 citations in OpenAlex.
- Scaling laws in confined media applied for biomarker detection.Nature communications · 2026Article
- Background-Free Nanopore Decoding of microRNA Expression Patterns Using Circular Diagnostic DNA.Analytical chemistry · 2026Article
- Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.ACS nano · 2025Article
- Real-Time Measurement of a Weak Interaction of a Transcription Factor Motif with a Protein Hub at Single-Molecule Precision.ACS nano · 2024Article
- Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel.International journal of molecular sciences · 2024Article
- Charged Biological Membranes Repel Large Neutral Molecules by Surface Dielectrophoresis and Counterion Pressure.Journal of the American Chemical Society · 2024Article
- Article
- A generalizable nanopore sensor for highly specific protein detection at single-molecule precision.Nature communications · 2023Article
- Assembly of transmembrane pores from mirror-image peptides.Nature communications · 2022Article
- Biological nanopores for single-molecule sensing.iScience · 2022Review
- Current noise of a protein-selective biological nanopore.Proteomics · 2022Article
- Disentangling the recognition complexity of a protein hub using a nanopore.Nature communications · 2022Article
- Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021Review
- Recent advances in biological nanopores for nanopore sequencing, sensing and comparison of functional variations in MspA mutants.RSC advances · 2021Review
- Nanopore Technology for the Application of Protein Detection.Nanomaterials (Basel, Switzerland) · 2021Review
- Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021Article
- Laser-based temperature control to study the roles of entropy and enthalpy in polymer-nanopore interactions.Science advances · 2021Article
- Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore.Nano letters · 2020Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Molecular crowding, a ubiquitous feature of the cellular environment, has significant implications in the kinetics and equilibrium of biopolymer interactions. In this study, a single charged polypeptide is exposed to competing forces that drive it into a transmembrane protein pore versus forces that pull it outside. Using single-molecule electrophysiology, we provide compelling experimental evidence that the kinetic details of the polypeptide-pore interactions are substantially affected by high concentrations of less-penetrating polyethylene glycols (PEGs). At a polymer concentration above a critical value, the presence of these neutral macromolecular crowders increases the rate constant of association but decreases the rate constant of dissociation, resulting in a stronger polypeptide-pore interaction. Moreover, a larger-molecular weight PEG exhibits a lower rate constant of association but a higher rate constant of dissociation than those values corresponding to a smaller-molecular weight PEG. These outcomes are in accord with a lower diffusion constant of the polypeptide and higher depletion-attraction forces between the polypeptide and transmembrane protein pore under crowding and confinement conditions.
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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.