Scaling Behavior of Ionic Transport in Membrane Nanochannels

Queralt-Martín, María; López, María Esther Álvarez; Aguilella‐Arzo, Marcel; Aguilella, Vicente M.; Alcaraz, Antonio

doi:10.1021/acs.nanolett.8b03235

Cited by 27 publications

(21 citation statements)

References 62 publications

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“…The conventional explanation of AMFE points to the correlated movement of ions in a single file fashion [ 19 ] characteristic of very narrow channels like gramicidin A [ 32 ]. However, E channel unitary conductance is similar to another multiionic proteolipidic pore, Alamethicin, in its lowest conductance state [ 9 , [33] , [34] , [35] ], which implies that it allows the transport of fully hydrated ions, water molecules and small molecules [ 22 ]. Since single-file transport of dehydrated ions seems highly improbable in multi-ionic pores such as synthetic nanopores where AMFE has already been reported [ 25 ], it has been suggested that AMFE may appear also because of localized, ion-specific binding within the pore [ 25 ].…”

Section: Resultsmentioning

confidence: 99%

Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance

Verdiá-Báguena

Aguilella

Queralt-Martín

et al. 2021

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The envelope protein E of the SARS-CoV coronavirus is an archetype of viroporin. It is a small hydrophobic protein displaying ion channel activity that has proven highly relevant in virus-host interaction and virulence. Ion transport through E channel was shown to alter Ca 2+ homeostasis in the cell and trigger inflammation processes. Here, we study transport properties of the E viroporin in mixed solutions of potassium and calcium chloride that contain a fixed total concentration (mole fraction experiments). The channel is reconstituted in planar membranes of different lipid compositions, including a lipid mixture that mimics the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane where the virus localizes within the cell. We find that the E ion conductance is non-monotonic with the total ionic concentration displaying an Anomalous Mole Fraction Effect (AMFE) only when charged lipids are present in the membrane. We also observe that E channel insertion in ERGIC-mimic membranes – including lipid with intrinsic negative curvature – enhances ion permeation at physiological concentrations of pure CaCl 2 or KCl solutions, with a preferential transport of Ca 2+ in mixed KCl-CaCl 2 solutions. Altogether, our findings demonstrate that the presence of calcium modulates the transport properties of the E channel by interacting preferentially with charged lipids through different mechanisms including direct Coulombic interactions and possibly inducing changes in membrane morphology.

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Section: Resultsmentioning

confidence: 99%

Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance

Verdiá-Báguena

Aguilella

Queralt-Martín

et al. 2021

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…To recapitulate, our results demonstrate the importance of lipid membrane composition in the mechanism of voltage-induced gating in large bacterial β-barrel channels. This adds to the number of central channel properties such as open channel current, selectivity, and interaction with partners that depend crucially on membrane composition [12,43,44,45,46,47,48,49]. In particular, we show unambiguously that lipid headgroup charge is an important modulator of OmpF gating, but it is not the only factor.…”

Section: Discussionmentioning

confidence: 60%

Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels

Perini

Alcaraz

Queralt-Martín

2019

IJMS

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The outer membrane of Gram-negative bacteria contains β-barrel proteins that form high-conducting ion channels providing a path for hydrophilic molecules, including antibiotics. Traditionally, these proteins have been considered to exist only in an open state so that regulation of outer membrane permeability was accomplished via protein expression. However, electrophysiological recordings show that β-barrel channels respond to transmembrane voltages by characteristically switching from a high-conducting, open state, to a so-called ‘closed’ state, with reduced permeability and possibly exclusion of large metabolites. Here, we use the bacterial porin OmpF from E. coli as a model system to gain insight on the control of outer membrane permeability by bacterial porins through the modulation of their open state. Using planar bilayer electrophysiology, we perform an extensive study of the role of membrane lipids in the OmpF channel closure by voltage. We pay attention not only to the effects of charges in the hydrophilic lipid heads but also to the contribution of the hydrophobic tails in the lipid-protein interactions. Our results show that gating kinetics is governed by lipid characteristics so that each stage of a sequential closure is different from the previous one, probably because of intra- or intermonomeric rearrangements.

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“…wileyonlinelibrary.com/journal/exploration  of  https://doi.org/10.1002/EXP.20210101 F I G U R E  Representative membrane structures for rational ion transport management, including nanochannel-structured membranes with single-dimensional nanochannels (i.e., 1D, 2D, and 3D) and mixed-dimensional nanochannels (i.e., 1D/1D, 1D/2D, 1D/3D, 2D/2D, 2D/3D, and 3D/3D), ultrathin membranes, and sandwich-like membranes, and their broad applications in the fields of ion separation, water purification, energy storage and conversion, sensors, and bioelectronics biological ion channel proteins [14][15][16][17][18][19][20][21] or artificial components with channels [22,23] in phospholipid bilayers. Reconstructed EcClC proteins embedded in lipid bilayers can function as H + and Cl − pumps with improved and controllable transport properties because of the superimposing or counterimposing gradients of H + and Cl − ions.…”

Section: Introductionmentioning

confidence: 99%

Rational ion transport management mediated through membrane structures

et al. 2021

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Unique membrane structures endow membranes with controlled ion transport properties in both biological and artificial systems, and they have shown broad application prospects from industrial production to biological interfaces. Herein, current advances in nanochannel‐structured membranes for manipulating ion transport are reviewed from the perspective of membrane structures. First, the controllability of ion transport through ion selectivity, ion gating, ion rectification, and ion storage is introduced. Second, nanochannel‐structured membranes are highlighted according to the nanochannel dimensions, including single‐dimensional nanochannels (i.e., 1D, 2D, and 3D) functioning by the controllable geometrical parameters of 1D nanochannels, the adjustable interlayer spacing of 2D nanochannels, and the interconnected ion diffusion pathways of 3D nanochannels, and mixed‐dimensional nanochannels (i.e., 1D/1D, 1D/2D, 1D/3D, 2D/2D, 2D/3D, and 3D/3D) tuned through asymmetric factors (e.g., components, geometric parameters, and interface properties). Then, ultrathin membranes with short ion transport distances and sandwich‐like membranes with more delicate nanochannels and combination structures are reviewed, and stimulus‐responsive nanochannels are discussed. Construction methods for nanochannel‐structured membranes are briefly introduced, and a variety of applications of these membranes are summarized. Finally, future perspectives to developing nanochannel‐structured membranes with unique structures (e.g., combinations of external macro/micro/nanostructures and the internal nanochannel arrangement) for mediating ion transport are presented.

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Scaling Behavior of Ionic Transport in Membrane Nanochannels

Cited by 27 publications

References 62 publications

Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance

Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance

Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels

Rational ion transport management mediated through membrane structures

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