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Visualizing Cyclic Peptide Hydration at the Single-Molecule Level

The role of water molecules in the selective transport of potassium ions across cell membranes is important. Experimental investigations of valinomycin–water interactions remain huge challenge due to the poor solubility of valinomycin in water. Herein, we removed this experimental obstacle by introd...

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Detalles Bibliográficos
Autores principales: Chen, Yumin, Deng, Ke, Qiu, Xiaohui, Wang, Chen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3746206/
https://www.ncbi.nlm.nih.gov/pubmed/23955234
http://dx.doi.org/10.1038/srep02461
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author Chen, Yumin
Deng, Ke
Qiu, Xiaohui
Wang, Chen
author_facet Chen, Yumin
Deng, Ke
Qiu, Xiaohui
Wang, Chen
author_sort Chen, Yumin
collection PubMed
description The role of water molecules in the selective transport of potassium ions across cell membranes is important. Experimental investigations of valinomycin–water interactions remain huge challenge due to the poor solubility of valinomycin in water. Herein, we removed this experimental obstacle by introducing gaseous water and valinomycin onto a Cu(111) surface to investigate the hydration of valinomycin. By combining scanning tunneling microscopy (STM) with density functional theory (DFT) calculations, we revealed that water could affect the adsorption structure of valinomycin. Hydrogen bond interactions occurred primarily at the carbonyl oxygen of valinomycin and resulted in the formation of valinomycin hydrates. The single-molecule perspective revealed in our investigation could provide new insight into the role of water on the conformation transition of valinomycin, which might provide a new molecular basis for the ion transport mechanism at the water/membrane interface.
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spelling pubmed-37462062013-08-19 Visualizing Cyclic Peptide Hydration at the Single-Molecule Level Chen, Yumin Deng, Ke Qiu, Xiaohui Wang, Chen Sci Rep Article The role of water molecules in the selective transport of potassium ions across cell membranes is important. Experimental investigations of valinomycin–water interactions remain huge challenge due to the poor solubility of valinomycin in water. Herein, we removed this experimental obstacle by introducing gaseous water and valinomycin onto a Cu(111) surface to investigate the hydration of valinomycin. By combining scanning tunneling microscopy (STM) with density functional theory (DFT) calculations, we revealed that water could affect the adsorption structure of valinomycin. Hydrogen bond interactions occurred primarily at the carbonyl oxygen of valinomycin and resulted in the formation of valinomycin hydrates. The single-molecule perspective revealed in our investigation could provide new insight into the role of water on the conformation transition of valinomycin, which might provide a new molecular basis for the ion transport mechanism at the water/membrane interface. Nature Publishing Group 2013-08-19 /pmc/articles/PMC3746206/ /pubmed/23955234 http://dx.doi.org/10.1038/srep02461 Text en Copyright © 2013, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/
spellingShingle Article
Chen, Yumin
Deng, Ke
Qiu, Xiaohui
Wang, Chen
Visualizing Cyclic Peptide Hydration at the Single-Molecule Level
title Visualizing Cyclic Peptide Hydration at the Single-Molecule Level
title_full Visualizing Cyclic Peptide Hydration at the Single-Molecule Level
title_fullStr Visualizing Cyclic Peptide Hydration at the Single-Molecule Level
title_full_unstemmed Visualizing Cyclic Peptide Hydration at the Single-Molecule Level
title_short Visualizing Cyclic Peptide Hydration at the Single-Molecule Level
title_sort visualizing cyclic peptide hydration at the single-molecule level
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3746206/
https://www.ncbi.nlm.nih.gov/pubmed/23955234
http://dx.doi.org/10.1038/srep02461
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