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Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor
Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007701/ https://www.ncbi.nlm.nih.gov/pubmed/33782419 http://dx.doi.org/10.1038/s41598-021-85015-w |
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author | Attia, Jessica Nir, Sivan Mervinetsky, Evgeniy Balogh, Dora Gitlin-Domagalska, Agata Alshanski, Israel Reches, Meital Hurevich, Mattan Yitzchaik, Shlomo |
author_facet | Attia, Jessica Nir, Sivan Mervinetsky, Evgeniy Balogh, Dora Gitlin-Domagalska, Agata Alshanski, Israel Reches, Meital Hurevich, Mattan Yitzchaik, Shlomo |
author_sort | Attia, Jessica |
collection | PubMed |
description | Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational change of the oxytocin peptide in the monolayer, which was measured using electrochemical impedance spectroscopy. Here, we demonstrate that sensing can be achieved also when the oxytocin is non-covalently integrated into an alkanethiol host monolayer. We show that ion-binding cause morphological changes to the dense host layer, which translates into enhanced impedimetric signals compared to direct covalent assembly strategies. This biosensor proved selective and sensitive for Zn(2+) ions in the range of nano- to micro-molar concentrations. This strategy offers an approach to utilize peptide flexibility in monitoring their response to the environment while embedded in a hydrophobic monolayer. |
format | Online Article Text |
id | pubmed-8007701 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-80077012021-03-30 Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor Attia, Jessica Nir, Sivan Mervinetsky, Evgeniy Balogh, Dora Gitlin-Domagalska, Agata Alshanski, Israel Reches, Meital Hurevich, Mattan Yitzchaik, Shlomo Sci Rep Article Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational change of the oxytocin peptide in the monolayer, which was measured using electrochemical impedance spectroscopy. Here, we demonstrate that sensing can be achieved also when the oxytocin is non-covalently integrated into an alkanethiol host monolayer. We show that ion-binding cause morphological changes to the dense host layer, which translates into enhanced impedimetric signals compared to direct covalent assembly strategies. This biosensor proved selective and sensitive for Zn(2+) ions in the range of nano- to micro-molar concentrations. This strategy offers an approach to utilize peptide flexibility in monitoring their response to the environment while embedded in a hydrophobic monolayer. Nature Publishing Group UK 2021-03-29 /pmc/articles/PMC8007701/ /pubmed/33782419 http://dx.doi.org/10.1038/s41598-021-85015-w Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Attia, Jessica Nir, Sivan Mervinetsky, Evgeniy Balogh, Dora Gitlin-Domagalska, Agata Alshanski, Israel Reches, Meital Hurevich, Mattan Yitzchaik, Shlomo Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor |
title | Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor |
title_full | Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor |
title_fullStr | Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor |
title_full_unstemmed | Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor |
title_short | Non-covalently embedded oxytocin in alkanethiol monolayer as Zn(2+) selective biosensor |
title_sort | non-covalently embedded oxytocin in alkanethiol monolayer as zn(2+) selective biosensor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007701/ https://www.ncbi.nlm.nih.gov/pubmed/33782419 http://dx.doi.org/10.1038/s41598-021-85015-w |
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