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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...

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Detalles Bibliográficos
Autores principales: Huang, Ao, Zhang, Luning, Li, Weiwei, Ma, Zeyu, Shuo, Shi, Yao, Tianming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society Publishing 2018
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
Descripción
Sumario: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.