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Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport
Transmembrane protein channels are of significant importance for the design of biomimetic artificial ion channels. Regarding the transport principles, they may be constructed from amphiphilic compounds undergoing self-assembly that synergistically generate directional superstructures across bilayer...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8134729/ https://www.ncbi.nlm.nih.gov/pubmed/34026736 http://dx.doi.org/10.3389/fchem.2021.678962 |
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author | Licsandru, Erol Andrei, Iuliana-Marilena van der Lee, Arie Barboiu, Mihail |
author_facet | Licsandru, Erol Andrei, Iuliana-Marilena van der Lee, Arie Barboiu, Mihail |
author_sort | Licsandru, Erol |
collection | PubMed |
description | Transmembrane protein channels are of significant importance for the design of biomimetic artificial ion channels. Regarding the transport principles, they may be constructed from amphiphilic compounds undergoing self-assembly that synergistically generate directional superstructures across bilayer membranes. Particularly interesting, these alignments may impose an artificial pore structure that may control the ionic conduction and translocate water and ions sharing one pathway across the cell membrane. Herein, we report that the imidazole and 3-amino-triazole amphiphiles self-assemble via multiple H-bonding to form stable artificial networks within lipid bilayers. The alignment of supramolecular assemblies influences the conduction of ions, envisioned to diffuse along the hydrophilic pathways. Compounds 1-8 present subtle variations on the ion transport activities, depending the structure of hydrophilic head and hydrophobic components. Fluorinated compounds 3, 4 and 7, 8 outperform the corresponding non-fluorinated counterparts 1, 2 and 5, 6. Under the same conditions, the R enantiomers present a higher activity vs. the S enantiomers. The present systems associating supramolecular self-assembly with ion-transport behaviors may represent very promising unexplored alternatives for ion-transport along with their transient superstructures within bilayer membranes, paralleling to that of biology. |
format | Online Article Text |
id | pubmed-8134729 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-81347292021-05-21 Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport Licsandru, Erol Andrei, Iuliana-Marilena van der Lee, Arie Barboiu, Mihail Front Chem Chemistry Transmembrane protein channels are of significant importance for the design of biomimetic artificial ion channels. Regarding the transport principles, they may be constructed from amphiphilic compounds undergoing self-assembly that synergistically generate directional superstructures across bilayer membranes. Particularly interesting, these alignments may impose an artificial pore structure that may control the ionic conduction and translocate water and ions sharing one pathway across the cell membrane. Herein, we report that the imidazole and 3-amino-triazole amphiphiles self-assemble via multiple H-bonding to form stable artificial networks within lipid bilayers. The alignment of supramolecular assemblies influences the conduction of ions, envisioned to diffuse along the hydrophilic pathways. Compounds 1-8 present subtle variations on the ion transport activities, depending the structure of hydrophilic head and hydrophobic components. Fluorinated compounds 3, 4 and 7, 8 outperform the corresponding non-fluorinated counterparts 1, 2 and 5, 6. Under the same conditions, the R enantiomers present a higher activity vs. the S enantiomers. The present systems associating supramolecular self-assembly with ion-transport behaviors may represent very promising unexplored alternatives for ion-transport along with their transient superstructures within bilayer membranes, paralleling to that of biology. Frontiers Media S.A. 2021-05-06 /pmc/articles/PMC8134729/ /pubmed/34026736 http://dx.doi.org/10.3389/fchem.2021.678962 Text en Copyright © 2021 Licsandru, Andrei, van der Lee and Barboiu. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Chemistry Licsandru, Erol Andrei, Iuliana-Marilena van der Lee, Arie Barboiu, Mihail Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport |
title | Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport |
title_full | Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport |
title_fullStr | Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport |
title_full_unstemmed | Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport |
title_short | Self-Assembled H-Bonding Superstructures for Alkali Cation and Proton Transport |
title_sort | self-assembled h-bonding superstructures for alkali cation and proton transport |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8134729/ https://www.ncbi.nlm.nih.gov/pubmed/34026736 http://dx.doi.org/10.3389/fchem.2021.678962 |
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