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Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein
We report an ultrasensitive immunoassay for tau protein—a key marker of Alzheimer's disease. This sensing platform relies on graphene oxide (GO) surfaces conjugated with anti-human tau antibody to provide quantitative binding sites for the tau protein. The GO quenches standard fluorescein isoth...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society Publishing
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5936912/ https://www.ncbi.nlm.nih.gov/pubmed/29765647 http://dx.doi.org/10.1098/rsos.171808 |
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author | Huang, Ao Zhang, Luning Li, Weiwei Ma, Zeyu Shuo, Shi Yao, Tianming |
author_facet | Huang, Ao Zhang, Luning Li, Weiwei Ma, Zeyu Shuo, Shi Yao, Tianming |
author_sort | Huang, Ao |
collection | PubMed |
description | We report an ultrasensitive immunoassay for tau protein—a key marker of Alzheimer's disease. This sensing platform relies on graphene oxide (GO) surfaces conjugated with anti-human tau antibody to provide quantitative binding sites for the tau protein. The GO quenches standard fluorescein isothiocyanate labelled tau (tau-FITC) when tau protein and tau-FITC are both present and compete for the binding sites. This change in fluorescence signal can be used to quantitate tau protein. In contrast with traditional enzyme-linked immunosorbent assay (ELISA), our method does not require enzyme-linked secondary antibodies for protein recognition nor does it require an enzyme substrate for optical signal generation. This requires fewer reagents and has less systematic error than the antigen–antibody recognition steps in ELISA. Our method has a tau protein detection limit of 0.14 pmol ml(−1) in buffer. This approach could be developed into a promising biosensor for the detection of tau protein and may be useful in the clinical diagnosis of tau-induced neurodegeneration syndromes. |
format | Online Article Text |
id | pubmed-5936912 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The Royal Society Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-59369122018-05-15 Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein Huang, Ao Zhang, Luning Li, Weiwei Ma, Zeyu Shuo, Shi Yao, Tianming R Soc Open Sci Chemistry We report an ultrasensitive immunoassay for tau protein—a key marker of Alzheimer's disease. This sensing platform relies on graphene oxide (GO) surfaces conjugated with anti-human tau antibody to provide quantitative binding sites for the tau protein. The GO quenches standard fluorescein isothiocyanate labelled tau (tau-FITC) when tau protein and tau-FITC are both present and compete for the binding sites. This change in fluorescence signal can be used to quantitate tau protein. In contrast with traditional enzyme-linked immunosorbent assay (ELISA), our method does not require enzyme-linked secondary antibodies for protein recognition nor does it require an enzyme substrate for optical signal generation. This requires fewer reagents and has less systematic error than the antigen–antibody recognition steps in ELISA. Our method has a tau protein detection limit of 0.14 pmol ml(−1) in buffer. This approach could be developed into a promising biosensor for the detection of tau protein and may be useful in the clinical diagnosis of tau-induced neurodegeneration syndromes. The Royal Society Publishing 2018-04-11 /pmc/articles/PMC5936912/ /pubmed/29765647 http://dx.doi.org/10.1098/rsos.171808 Text en © 2018 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Chemistry Huang, Ao Zhang, Luning Li, Weiwei Ma, Zeyu Shuo, Shi Yao, Tianming Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
title | Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
title_full | Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
title_fullStr | Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
title_full_unstemmed | Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
title_short | Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
title_sort | controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5936912/ https://www.ncbi.nlm.nih.gov/pubmed/29765647 http://dx.doi.org/10.1098/rsos.171808 |
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