Controlled fluorescence quenching by antibody-conjugated graphene oxide to measure tau protein

被引:36
|
作者
Huang, Ao [1 ]
Zhang, Luning [1 ]
Li, Weiwei [1 ]
Ma, Zeyu [1 ]
Shuo, Shi [1 ]
Yao, Tianming [1 ]
机构
[1] Tongji Univ, Sch Chem Sci & Engn, 1239 Siping Rd, Shanghai 200092, Peoples R China
来源
ROYAL SOCIETY OPEN SCIENCE | 2018年 / 5卷 / 04期
基金
中国国家自然科学基金;
关键词
tau protein; Alzheimer's disease; biosensor; graphene oxide; immunoassay; LINKED-IMMUNOSORBENT-ASSAY; RESONANCE ENERGY-TRANSFER; ALZHEIMERS-DISEASE; MONOCLONAL-ANTIBODY; ULTRASENSITIVE DETECTION; HOMOGENEOUS IMMUNOASSAY; CEREBROSPINAL-FLUID; LABEL; SERS; BIOMARKERS;
D O I
10.1098/rsos.171808
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
We report an ultrasensitive immunoassay for tau protein-a keymarker 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.
引用
收藏
页数:10
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