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Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins
BACKGROUND: Construction of electrochemical impedance sensors by the self-assembly technique has become a promising strategy for the ‘label-free’ detection of protein-ligand interactions. However, previous impedance sensors are devoid of an inherent electrochemical signal, which limits the standardi...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4245500/ https://www.ncbi.nlm.nih.gov/pubmed/25435901 http://dx.doi.org/10.1186/s13065-014-0067-y |
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author | Zhu, Bi-Wen Cai, Liang He, Xiao-Peng Chen, Guo-Rong Long, Yi-Tao |
author_facet | Zhu, Bi-Wen Cai, Liang He, Xiao-Peng Chen, Guo-Rong Long, Yi-Tao |
author_sort | Zhu, Bi-Wen |
collection | PubMed |
description | BACKGROUND: Construction of electrochemical impedance sensors by the self-assembly technique has become a promising strategy for the ‘label-free’ detection of protein-ligand interactions. However, previous impedance sensors are devoid of an inherent electrochemical signal, which limits the standardization of the sensors for protein recognition in a reproducible manner. RESULTS: We designed and synthesized an anthraquinonyl glycoside (AG) where the anthraquinone (AQ) moiety can bind to the surface of a graphene-based working electrode while the glycoside serving as a ligand for lectin. By measuring the inherent voltammetric signal of AQ, the glycosides decorated on the working electrode could be simply quantified to obtain electrodes with a unified signal window. Subsequently, impedance analysis showed that the ‘standardized’ electrodes gave a reproducible electrochemical response to a selective lectin with no signal variation in the presence of unselective proteins. CONCLUSION: Anthraquinone-modified ligands could be used to facilitate the standardization of electrochemical impedance sensors for the reproducible, selective analysis of ligand-protein interactions. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13065-014-0067-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4245500 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-42455002014-11-28 Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins Zhu, Bi-Wen Cai, Liang He, Xiao-Peng Chen, Guo-Rong Long, Yi-Tao Chem Cent J Research Article BACKGROUND: Construction of electrochemical impedance sensors by the self-assembly technique has become a promising strategy for the ‘label-free’ detection of protein-ligand interactions. However, previous impedance sensors are devoid of an inherent electrochemical signal, which limits the standardization of the sensors for protein recognition in a reproducible manner. RESULTS: We designed and synthesized an anthraquinonyl glycoside (AG) where the anthraquinone (AQ) moiety can bind to the surface of a graphene-based working electrode while the glycoside serving as a ligand for lectin. By measuring the inherent voltammetric signal of AQ, the glycosides decorated on the working electrode could be simply quantified to obtain electrodes with a unified signal window. Subsequently, impedance analysis showed that the ‘standardized’ electrodes gave a reproducible electrochemical response to a selective lectin with no signal variation in the presence of unselective proteins. CONCLUSION: Anthraquinone-modified ligands could be used to facilitate the standardization of electrochemical impedance sensors for the reproducible, selective analysis of ligand-protein interactions. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13065-014-0067-y) contains supplementary material, which is available to authorized users. Springer International Publishing 2014-11-25 /pmc/articles/PMC4245500/ /pubmed/25435901 http://dx.doi.org/10.1186/s13065-014-0067-y Text en © Zhu et al.; licensee Springer. 2014 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Zhu, Bi-Wen Cai, Liang He, Xiao-Peng Chen, Guo-Rong Long, Yi-Tao Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
title | Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
title_full | Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
title_fullStr | Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
title_full_unstemmed | Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
title_short | Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
title_sort | anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4245500/ https://www.ncbi.nlm.nih.gov/pubmed/25435901 http://dx.doi.org/10.1186/s13065-014-0067-y |
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