Synthetic models of cation-conducting channels

Gokel, George W.; Mukhopadhyay, Amartya

doi:10.1039/b008667n

Cited by 258 publications

(192 citation statements)

References 36 publications

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“…1). Their rare characteristics compared to the other synthetic ion channels/pores, [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23] i.e. the possibility to install functional groups along the ion-conducting pathway, encouraged the shift of our interest from biomimicry to practical applications.…”

Section: Introductionmentioning

confidence: 99%

Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH

et al. 2003

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We report the characterization of multifunctional rigid-rod β-barrel ion channels with either internal aspartates or arginine-histidine dyads by planar bilayer conductance experiments. Barrels with internal aspartates form cation selective, large, unstable and ohmic barrel-stave (rather than toroidal) pores; addition of magnesium cations nearly deletes cation selectivity and increases single-channel stability. Barrels with internal arginine-histidine dyads form cation selective (P K ϩ/P Cl Ϫ = 2.1), small and ohmic ion channels with superb stability (single-channel lifetime > 20 seconds). Addition of "protons" results in inversion of anion/cation selectivity (P Cl Ϫ/P K ϩ = 3.8); addition of an anionic guest (HPTS) results in the blockage of anion selective but not cation selective channels. These results suggest that specific, internal counterion immobilization, here magnesium (but not sodium or potassium) cations by internal aspartates and inorganic phosphates by internal arginines (but not histidines), provides access to synthetic multifunctional pores with attractive properties.

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Section: Introductionmentioning

confidence: 99%

Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH

et al. 2003

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“…), pointing toward the protein ion-transporting core, surrounded by the outer scaffolding protein wall orienting the transport direction. Artificial bilayer (6)(7)(8)(9)(10) or nanotube membrane systems (11)(12)(13)(14) were developed during the last decades with the hope of mimicking the natural ion channels, to the direct benefit of the fields of chemical separations, sensors, or storage-delivery devices. Self-assembly is an elegant approach to constructing synthetic ion channels.…”

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confidence: 99%

Dynamic hybrid materials for constitutional self-instructed membranes

Cazacu

Legrand

Pasc

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Constitutional self-instructed membranes were developed and used for mimicking the adaptive structural functionality of natural ionchannel systems. These membranes are based on dynamic hybrid materials in which the functional self-organized macrocycles are reversibly connected with the inorganic silica through hydrophobic noncovalent interactions. Supramolecular columnar ion-channel architectures can be generated by reversible confinement within scaffolding hydrophobic silica mesopores. They can be structurally determined by using X-ray diffraction and morphologically tuned by alkali-salts templating. From the conceptual point of view, these membranes express a synergistic adaptive behavior: the simultaneous binding of the fittest cation and its anion would be a case of ''homotropic allosteric interactions,'' because in time it increases the transport efficiency of the pore-contained superstructures by a selective evolving process toward the fittest ion channel. The hybrid membranes presented here represent dynamic constitutional systems evolving over time to form the fittest ion channels from a library of molecular and supramolecular components, or selecting the fittest ion pairs from a mixture of salts demonstrating flexible adaptation.crown-ethers ͉ ion channels ͉ self-assembly

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“…We have recently reviewed the development of channel models [31] [32], so only a brief recounting of the history will be presented here. The earliest non-peptidic, synthetic organic channel model was reported by Tabushi, Kuroda, and Yokota [33].…”

Section: Non-peptide Channel Modelsmentioning

confidence: 99%

Synthetic, Biologically Active Amphiphilic Peptides

Yamnitz

Gokel

2007

Chemistry & Biodiversity

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Amphiphilic peptides typically consist of a peptide portion that may be 5-25 (or more) amino acids in length. The hydrophobic portion may be a single fatty acid residue, but can also be more elaborate. The main focus of this article lies on the family of synthetic anion binders (SATs) of the general structure (R 1 ) 2 N-COCH 2 OCH 2 CO-(Aaa) n -OR 3 . The most-common R 1 groups are octadecyl (C 18 H 37 ). The most studied peptide sequence in this family is (Gly) 3 -Pro-(Gly) 3 , although different sequences (and longer and shorter peptides) have been prepared as well. The C-terminal ester residue providing the most effective anion release from liposomes is heptyl (C 7 H 15 ), although many others have been examined. The compound (C 18 H 37 ) 2 N-COCH 2 OCH 2 CO-(Gly) 3 -Pro-(Gly) 3 -OBn (Bn=benzyl) was found to mediate Cl -transport in mouse epithelial cells.

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Synthetic models of cation-conducting channels

Cited by 258 publications

References 36 publications

Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH

Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH

Dynamic hybrid materials for constitutional self-instructed membranes

Synthetic, Biologically Active Amphiphilic Peptides

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