ArticleProceedings of the National Academy of Sciences of the United States of America2016
Size-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Coil-Globule versus Field-Driven Coil-Blob Transitions of PEG under Nanopore Confinement.ACS measurement science au · 2026Article
- Geometric Confinement in Solid-State Nanopores Enables Single-Molecule Discrimination of Ferritin Subunits and Translocation Bias.Nano letters · 2026Article
- Recent Advances in Mitochondria-Targeted Nano-Drug Delivery Systems for Cancer Therapy.International journal of nanomedicine · 2026Review
- Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins.Science advances · 2025Article
- Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins.Nature communications · 2024Article
- Targeting mitochondrial ion channels for cancer therapy.Redox biology · 2021Review
- Design and Assembly of Transmembrane Helix Barrel.The Journal of membrane biology · 2020Article
- Article
- FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution.Nature communications · 2019Article
- Poly(ethylene glycol)s in Semidilute Regime: Radius of Gyration in the Bulk and Partitioning into a Nanopore.Macromolecules · 2017Article
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Authors and funding
6 authors.
Funding
Abstract
Nonideal polymer mixtures of PEGs of different molecular weights partition differently into nanosize protein channels. Here, we assess the validity of the recently proposed theoretical approach of forced partitioning for three structurally different β-barrel channels: voltage-dependent anion channel from outer mitochondrial membrane VDAC, bacterial porin OmpC (outer membrane protein C), and bacterial channel-forming toxin α-hemolysin. Our interpretation is based on the idea that relatively less-penetrating polymers push the more easily penetrating ones into nanosize channels in excess of their bath concentration. Comparison of the theory with experiments is excellent for VDAC. Polymer partitioning data for the other two channels are consistent with theory if additional assumptions regarding the energy penalty of pore penetration are included. The obtained results demonstrate that the general concept of "polymers pushing polymers" is helpful in understanding and quantification of concrete examples of size-dependent forced partitioning of polymers into protein nanopores.
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