ArticleBiophysical journal2003
Partitioning of individual flexible polymers into a nanoscopic protein pore.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Probing Voltage Dependence Interaction of Cationic Peptides with Bacterial Porins at A Single-Molecule Level.Cell biochemistry and biophysics · 2026Article
- Coil-Globule versus Field-Driven Coil-Blob Transitions of PEG under Nanopore Confinement.ACS measurement science au · 2026Article
- Scaling laws in confined media applied for biomarker detection.Nature communications · 2026Article
- Article
- Revealing the single-channel characteristics of OprD (OccAB1) porins from hospital strains of Acinetobacter baumannii.European biophysics journal : EBJ · 2023Article
- Identification of tagged glycans with a protein nanopore.Nature communications · 2023Article
- About the Influence of PEG Spacers on the Cytotoxicity of Titanate Nanotubes-Docetaxel Nanohybrids against a Prostate Cancer Cell Line.Nanomaterials (Basel, Switzerland) · 2021Article
- Laser-based temperature control to study the roles of entropy and enthalpy in polymer-nanopore interactions.Science advances · 2021Article
- Article
- Size-dependent interaction of a 3-arm star poly(ethylene glycol) with two biological nanopores.The European physical journal. E, Soft matter · 2018Article
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- Poly(ethylene glycol)s in Semidilute Regime: Radius of Gyration in the Bulk and Partitioning into a Nanopore.Macromolecules · 2017Article
- MOSAIC: A Modular Single-Molecule Analysis Interface for Decoding Multistate Nanopore Data.Analytical chemistry · 2016Article
- Article
- Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Revealing different aggregational states of a conjugated polymer in solution by a nanopore sensor.Chemical science · 2016Article
- Forces from the Portal Govern the Late-Stage DNA Transport in a Viral DNA Packaging Nanomotor.Biophysical journal · 2016Article
- Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore.Scientific reports · 2016Article
- Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016Article
- Semisynthetic protein nanoreactor for single-molecule chemistry.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polymer dynamics are of fundamental importance in materials science, biotechnology, and medicine. However, very little is known about the kinetics of partitioning of flexible polymer molecules into pores of nanometer dimensions. We employed electrical recording to probe the partitioning of single poly(ethylene glycol) (PEG) molecules, at concentrations near the dilute regime, into the transmembrane beta-barrel of individual protein pores formed from staphylococcal alpha-hemolysin (alphaHL). The interactions of the alpha-hemolysin pore with the PEGs (M(w) 940-6000 Da) fell into two classes: short-duration events (tau approximately 20 micro s), approximately 85% of the total, and long-duration events (tau approximately 100 micro s), approximately 15% of the total. The association rate constants (k(on)) for both classes of events were strongly dependent on polymer mass, and values of k(on) ranged over two orders of magnitude. By contrast, the dissociation rate constants (k(off)) exhibited a weak dependence on mass, suggesting that the polymer chains are largely compacted before they enter the pore, and do not decompact to a significant extent before they exit. The values of k(on) and k(off) were used to determine partition coefficients (Pi) for the PEGs between the bulk aqueous phase and the pore lumen. The low values of Pi are in keeping with a negligible interaction between the PEG chains and the interior surface of the pore, which is independent of ionic strength. For the long events, values of Pi decrease exponentially with polymer mass, according to the scaling law of Daoud and de Gennes. For PEG molecules larger than approximately 5 kDa, Pi reached a limiting value suggesting that these PEG chains cannot fit entirely into the beta-barrel.
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