ArticleBiophysical journal2009
Diffusion, exclusion, and specific binding in a large channel: a study of OmpF selectivity inversion.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 91 citations in OpenAlex.
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- Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.Nature communications · 2023Article
- The Complex Proteolipidic Behavior of the SARS-CoV-2 Envelope Protein Channel: Weak Selectivity and Heterogeneous Oligomerization.International journal of molecular sciences · 2023Article
- Surface-Functionalized Polystyrene Nanoparticles Alter the Transmembrane Potential via Ion-Selective Pores Maintaining Global Bilayer Integrity.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- The P. aeruginosa effector Tse5 forms membrane pores disrupting the membrane potential of intoxicated bacteria.Communications biology · 2022Article
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- Dynorphin A induces membrane permeabilization by formation of proteolipidic pores. Insights from electrophysiology and computational simulations.Computational and structural biotechnology journal · 2022Article
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- A pH-independent quiet OmpG pore with enhanced electrostatic repulsion among the extracellular loops.Biochimica et biophysica acta. Biomembranes · 2021Article
- A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology.The Journal of general physiology · 2020Article
- Effect of late endosomal DOBMP lipid and traditional model lipids of electrophysiology on the anthrax toxin channel activity.Biochimica et biophysica acta. Biomembranes · 2018Article
- Scaling Behavior of Ionic Transport in Membrane Nanochannels.Nano letters · 2018Article
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- Understanding antibiotic resistance via outer membrane permeability.Infection and drug resistance · 2018Review
- On the different sources of cooperativity in pH titrating sites of a membrane protein channel.The European physical journal. E, Soft matter · 2016Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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Abstract
We find that moderate cationic selectivity of the general bacterial porin OmpF in sodium and potassium chloride solutions is inversed to anionic selectivity in concentrated solutions of barium, calcium, nickel, and magnesium chlorides. To understand the origin of this phenomenon, we consider several factors, which include the binding of divalent cations, electrostatic and steric exclusion of differently charged and differently sized ions, size-dependent hydrodynamic hindrance, electrokinetic effects, and significant "anionic" diffusion potential for bulk solutions of chlorides of divalent cations. Though all these factors contribute to the measured selectivity of this large channel, the observed selectivity inversion is mostly due to the following two. First, binding divalent cations compensates, or even slightly overcompensates, for the negative charge of the OmpF protein, which is known to be the main cause of cationic selectivity in sodium and potassium chloride solutions. Second, the higher anionic (versus cationic) transport rate expected for bulk solutions of chloride salts of divalent cations is the leading cause of the measured anionic selectivity of the channel. Interestingly, at high concentrations the binding of cations does not show any pronounced specificity within the divalent series because the reversal potentials measured in the series correlate well with the corresponding bulk diffusion potentials. Thus our study shows that, in contrast to the highly selective channels of neurophysiology that employ mostly the exclusion mechanism, quite different factors account for the selectivity of large channels. The elucidation of these factors is essential for understanding large channel selectivity and its regulation in vivo.
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