ArticleChemistry Central journal2014
Anthraquinonyl glycoside facilitates the standardization of graphene electrodes for the impedance detection of lectins.
Article in Chemistry Central journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Carbon-based glyco-nanoplatforms: towards the next generation of glycan-based multivalent probes.Chemical Society reviews · 2022Review
- Glycan-Based Electrochemical Biosensors: Promising Tools for the Detection of Infectious Diseases and Cancer Biomarkers.Molecules (Basel, Switzerland) · 2022Review
- A Graphene-Based Glycan Biosensor for Electrochemical Label-Free Detection of a Tumor-Associated Antibody.Sensors (Basel, Switzerland) · 2019Article
- Dynamic tracking of pathogenic receptor expression of live cells using pyrenyl glycoanthraquinone-decorated graphene electrodes.Chemical science · 2015Article
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Authors and funding
5 authors.
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Abstract
backgroundConstruction 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.
resultsWe 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.
conclusionAnthraquinone-modified ligands could be used to facilitate the standardization of electrochemical impedance sensors for the reproducible, selective analysis of ligand-protein interactions.
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