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Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns

Diverse classes of anion transporters have been developed, most of which focus on the transmembrane chloride transport due to its significance in living systems. Fluoride transport has, to some extent, been overlooked despite the importance of fluoride channels in bacterial survival. Here, we report...

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Autores principales: Zhao, Zhixing, Zhang, Miaomiao, Tang, Bailing, Weng, Peimin, Zhang, Yueyang, Yan, Xiaosheng, Li, Zhao, Jiang, Yun-Bao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7835674/
https://www.ncbi.nlm.nih.gov/pubmed/33511101
http://dx.doi.org/10.3389/fchem.2020.621323
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author Zhao, Zhixing
Zhang, Miaomiao
Tang, Bailing
Weng, Peimin
Zhang, Yueyang
Yan, Xiaosheng
Li, Zhao
Jiang, Yun-Bao
author_facet Zhao, Zhixing
Zhang, Miaomiao
Tang, Bailing
Weng, Peimin
Zhang, Yueyang
Yan, Xiaosheng
Li, Zhao
Jiang, Yun-Bao
author_sort Zhao, Zhixing
collection PubMed
description Diverse classes of anion transporters have been developed, most of which focus on the transmembrane chloride transport due to its significance in living systems. Fluoride transport has, to some extent, been overlooked despite the importance of fluoride channels in bacterial survival. Here, we report the design and synthesis of a cyclic azapeptide (a peptide-based N-amidothiourea, 1), as a transporter for fluoride transportation through a confined cavity that encapsulates fluoride, together with acyclic control compounds, the analogs 2 and 3. Cyclic receptor 1 exhibits more stable β-turn structures than the control compounds 2 and 3 and affords a confined cavity containing multiple inner –NH protons that serve as hydrogen bond donors to bind anions. It is noteworthy that the cyclic receptor 1 shows the capacity to selectively transport fluoride across a lipid bilayer on the basis of the osmotic and fluoride ion-selective electrode (ISE) assays, during which an electrogenic anion transport mechanism is found operative, whereas no transmembrane transport activity was found with 2 and 3, despite the fact that 2 and 3 are also able to bind fluoride via the thiourea moieties. These results demonstrate that the encapsulation of an anionic guest within a cyclic host compound is key to enhancing the anion transport activity and selectivity.
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spelling pubmed-78356742021-01-27 Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns Zhao, Zhixing Zhang, Miaomiao Tang, Bailing Weng, Peimin Zhang, Yueyang Yan, Xiaosheng Li, Zhao Jiang, Yun-Bao Front Chem Chemistry Diverse classes of anion transporters have been developed, most of which focus on the transmembrane chloride transport due to its significance in living systems. Fluoride transport has, to some extent, been overlooked despite the importance of fluoride channels in bacterial survival. Here, we report the design and synthesis of a cyclic azapeptide (a peptide-based N-amidothiourea, 1), as a transporter for fluoride transportation through a confined cavity that encapsulates fluoride, together with acyclic control compounds, the analogs 2 and 3. Cyclic receptor 1 exhibits more stable β-turn structures than the control compounds 2 and 3 and affords a confined cavity containing multiple inner –NH protons that serve as hydrogen bond donors to bind anions. It is noteworthy that the cyclic receptor 1 shows the capacity to selectively transport fluoride across a lipid bilayer on the basis of the osmotic and fluoride ion-selective electrode (ISE) assays, during which an electrogenic anion transport mechanism is found operative, whereas no transmembrane transport activity was found with 2 and 3, despite the fact that 2 and 3 are also able to bind fluoride via the thiourea moieties. These results demonstrate that the encapsulation of an anionic guest within a cyclic host compound is key to enhancing the anion transport activity and selectivity. Frontiers Media S.A. 2021-01-12 /pmc/articles/PMC7835674/ /pubmed/33511101 http://dx.doi.org/10.3389/fchem.2020.621323 Text en Copyright © 2021 Zhao, Zhang, Tang, Weng, Zhang, Yan, Li and Jiang. http://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
Zhao, Zhixing
Zhang, Miaomiao
Tang, Bailing
Weng, Peimin
Zhang, Yueyang
Yan, Xiaosheng
Li, Zhao
Jiang, Yun-Bao
Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
title Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
title_full Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
title_fullStr Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
title_full_unstemmed Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
title_short Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
title_sort transmembrane fluoride transport by a cyclic azapeptide with two β-turns
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7835674/
https://www.ncbi.nlm.nih.gov/pubmed/33511101
http://dx.doi.org/10.3389/fchem.2020.621323
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