Imidazole derivatives as artificial water channel building-blocks: structural design influence on water permeability

2018 ◽  
Vol 209 ◽  
pp. 113-124 ◽  
Author(s):  
Zhanhu Sun ◽  
Istvan Kocsis ◽  
Yuhao Li ◽  
Yves-Marie Legrand ◽  
Mihail Barboiu

A series of mono- and di-ureidoethylimidazole derivatives were tested as self-assembled supramolecular channels for water transport across a vesicle bilayer. Structural modifications of the selected compounds were related to permeability variation.


Membranes ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 646
Author(s):  
Hao-Chen Wu ◽  
Tomohisa Yoshioka ◽  
Keizo Nakagawa ◽  
Takuji Shintani ◽  
Hideto Matsuyama

The use of an Amphotericin B_Ergosterol (AmBEr) channel as an artificial water channel in forward osmosis filtration (FO) was studied via molecular dynamics (MD) simulation. Three channel models were constructed: a common AmBEr channel and two modified C3deOAmB_Ergosterol (C3deOAmBEr) channels with different diameters (12 Å and 18 Å). During FO filtration simulation, the osmotic pressure of salt-water was a driving force for water permeation. We examined the effect of the modified C3deOAmBEr channel on the water transport performance. By tracing the change of the number of water molecules along with simulation time in the saltwater region, the water permeability of the channel models could be calculated. A higher water permeability was observed for a modified C3deOAmBEr channel, and there was no ion permeation during the entire simulation period. The hydrated ions and water molecules were placed into the channel to explore the ion leakage behavior of the channels. The mean squared displacement (MSD) of ions and water molecules was obtained to study the ion leakage performance. The Amphotericin B-based channels showed excellent selectivity of water molecules against ions. The results obtained on an atomistic scale could assist in determining the properties and the optimal filtration applications for Amphotericin B-based channels.



2001 ◽  
Vol 276 (15) ◽  
pp. 12147-12152 ◽  
Author(s):  
Fabiana Garcı́a ◽  
Arlinet Kierbel ◽  
M. Cecilia Larocca ◽  
Sergio A. Gradilone ◽  
Patrick Splinter ◽  
...  

We previously found that water transport across hepatocyte plasma membranes occurs mainly via a non-channel mediated pathway. Recently, it has been reported that mRNA for the water channel, aquaporin-8 (AQP8), is present in hepatocytes. To further explore this issue, we studied protein expression, subcellular localization, and regulation of AQP8 in rat hepatocytes. By subcellular fractionation and immunoblot analysis, we detected anN-glycosylated band of ∼34 kDa corresponding to AQP8 in hepatocyte plasma and intracellular microsomal membranes. Confocal immunofluorescence microscopy for AQP8 in cultured hepatocytes showed a predominant intracellular vesicular localization. Dibutyryl cAMP (Bt2cAMP) stimulated the redistribution of AQP8 to plasma membranes. Bt2cAMP also significantly increased hepatocyte membrane water permeability, an effect that was prevented by the water channel blocker dimethyl sulfoxide. The microtubule blocker colchicine but not its inactive analog lumicolchicine inhibited the Bt2cAMP effect on both AQP8 redistribution to cell surface and hepatocyte membrane water permeability. Our data suggest that in rat hepatocytes AQP8 is localized largely in intracellular vesicles and can be redistributed to plasma membranes via a microtubule-depending, cAMP-stimulated mechanism. These studies also suggest that aquaporins contribute to water transport in cAMP-stimulated hepatocytes, a process that could be relevant to regulated hepatocyte bile secretion.



2012 ◽  
Vol 141 (1) ◽  
pp. 119-132 ◽  
Author(s):  
Byung-Ju Jin ◽  
Hua Zhang ◽  
Devin K. Binder ◽  
A.S. Verkman

Potassium (K+) ions released into brain extracellular space (ECS) during neuroexcitation are efficiently taken up by astrocytes. Deletion of astrocyte water channel aquaporin-4 (AQP4) in mice alters neuroexcitation by reducing ECS [K+] accumulation and slowing K+ reuptake. These effects could involve AQP4-dependent: (a) K+ permeability, (b) resting ECS volume, (c) ECS contraction during K+ reuptake, and (d) diffusion-limited water/K+ transport coupling. To investigate the role of these mechanisms, we compared experimental data to predictions of a model of K+ and water uptake into astrocytes after neuronal release of K+ into the ECS. The model computed the kinetics of ECS [K+] and volume, with input parameters including initial ECS volume, astrocyte K+ conductance and water permeability, and diffusion in astrocyte cytoplasm. Numerical methods were developed to compute transport and diffusion for a nonstationary astrocyte–ECS interface. The modeling showed that mechanisms b–d, together, can predict experimentally observed impairment in K+ reuptake from the ECS in AQP4 deficiency, as well as altered K+ accumulation in the ECS after neuroexcitation, provided that astrocyte water permeability is sufficiently reduced in AQP4 deficiency and that solute diffusion in astrocyte cytoplasm is sufficiently low. The modeling thus provides a potential explanation for AQP4-dependent K+/water coupling in the ECS without requiring AQP4-dependent astrocyte K+ permeability. Our model links the physical and ion/water transport properties of brain cells with the dynamics of neuroexcitation, and supports the conclusion that reduced AQP4-dependent water transport is responsible for defective neuroexcitation in AQP4 deficiency.



Author(s):  
Serena Gentile ◽  
Erica Del Grosso ◽  
Leonard J. Prins ◽  
Francesco Ricci


Nanoscale ◽  
2021 ◽  
Author(s):  
Michael Penth ◽  
Kordula Schellnhuber ◽  
Roland Bennewitz ◽  
Johanna Blass

Massive parallel force spectroscopy reveals a surprisingly high flexibility for DNA constructs used in DNA origami. The high flexibility is attributed to the structural dynamics of DNA self-assemblies.



Soft Matter ◽  
2021 ◽  
Author(s):  
Jiawei Lu ◽  
Xiangyu Bu ◽  
Xinghua Zhang ◽  
Bing Liu

The shapes of colloidal particles are crucial to the self-assembled superstructures. Understanding the relationship between the shapes of building blocks and the resulting crystal structures is an important fundamental question....



Science ◽  
2020 ◽  
Vol 371 (6524) ◽  
pp. 72-75 ◽  
Author(s):  
Tyler E. Culp ◽  
Biswajit Khara ◽  
Kaitlyn P. Brickey ◽  
Michael Geitner ◽  
Tawanda J. Zimudzi ◽  
...  

Biological membranes can achieve remarkably high permeabilities, while maintaining ideal selectivities, by relying on well-defined internal nanoscale structures in the form of membrane proteins. Here, we apply such design strategies to desalination membranes. A series of polyamide desalination membranes—which were synthesized in an industrial-scale manufacturing line and varied in processing conditions but retained similar chemical compositions—show increasing water permeability and active layer thickness with constant sodium chloride selectivity. Transmission electron microscopy measurements enabled us to determine nanoscale three-dimensional polyamide density maps and predict water permeability with zero adjustable parameters. Density fluctuations are detrimental to water transport, which makes systematic control over nanoscale polyamide inhomogeneity a key route to maximizing water permeability without sacrificing salt selectivity in desalination membranes.





1996 ◽  
Vol 270 (1) ◽  
pp. C12-C30 ◽  
Author(s):  
A. S. Verkman ◽  
A. N. van Hoek ◽  
T. Ma ◽  
A. Frigeri ◽  
W. R. Skach ◽  
...  

This review summarizes recent progress in water-transporting mechanisms across cell membranes. Modern biophysical concepts of water transport and new measurement strategies are evaluated. A family of water-transporting proteins (water channels, aquaporins) has been identified, consisting of small hydrophobic proteins expressed widely in epithelial and nonepithelial tissues. The functional properties, genetics, and cellular distributions of these proteins are summarized. The majority of molecular-level information about water-transporting mechanisms comes from studies on CHIP28, a 28-kDa glycoprotein that forms tetramers in membranes; each monomer contains six putative helical domains surrounding a central aqueous pathway and functions independently as a water-selective channel. Only mutations in the vasopressin-sensitive water channel have been shown to cause human disease (non-X-linked congenital nephrogenic diabetes insipidus); the physiological significance of other water channels remains unproven. One mercurial-insensitive water channel has been identified, which has the unique feature of multiple overlapping transcriptional units. Systems for expression of water channel proteins are described, including Xenopus oocytes, mammalian and insect cells, and bacteria. Further work should be directed at elucidation of the role of water channels in normal physiology and disease, molecular analysis of regulatory mechanisms, and water channel structure determination at atomic resolution.



Carbon ◽  
2017 ◽  
Vol 118 ◽  
pp. 458-466 ◽  
Author(s):  
V. Boffa ◽  
H. Etmimi ◽  
P.E. Mallon ◽  
H.Z. Tao ◽  
G. Magnacca ◽  
...  


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