A photoelectrochemical immunosensor based on CdS/CdTe-cosensitized SnO2 as a platform for the ultrasensitive detection of amyloid β-protein

The Analyst ◽  
2020 ◽  
Vol 145 (2) ◽  
pp. 619-625 ◽  
Author(s):  
Nuo Zhang ◽  
Yaoguang Wang ◽  
Guanhui Zhao ◽  
Chao Wang ◽  
Yueyuan Li ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Ultrasensitive Detection ◽  
Amyloid Β Protein ◽  
Label Free ◽  
Β Protein

An ultrasensitive label-free photoelectrochemical immunosensor was developed to detect amyloid β-protein based on CdS/CdTe-cosensitized SnO2 nanoflowers.

scholarly journals Bioinspired Synthesis of ZnO@polydopamine/Au for Label-Free Photoelectrochemical Immunoassay of Amyloid-β Protein

2021 ◽  
Vol 9 ◽  
Author(s):  
Guangli He ◽  
Yue Zhou ◽  
Mifang Li ◽  
Yanzhen Guo ◽  
Hang Yin ◽  
...  
Keyword(s):  
Visible Light ◽  
Early Stage ◽  
Resonance Effect ◽  
Amyloid Β ◽  
Localized Surface Plasmon ◽  
Quantitative Detection ◽  
Amyloid Β Protein ◽  
Label Free ◽  
Au Nps ◽  
Β Protein

Amyloid-β protein (Aβ) is an important biomarker and plays a key role in the early stage of Alzheimer’s disease (AD). Here, an ultrasensitive photoelectrochemical (PEC) sensor based on ZnO@polydopamine/Au nanocomposites was constructed for quantitative detection of Aβ. In this sensing system, the ZnO nanorod array decorated with PDA films and gold nanoparticles (Au NPs) have excellent visible-light activity. The PDA film was used as a sensitizer for charge separation, and it also was used for antibody binding. Moreover, Au NPs were loaded on the surface of PDA film by in situ deposition, which further improved the charge transfer efficiency and the PEC activity in visible light due to the localized surface plasmon resonance effect of Au NPs. Therefore, in ZnO@polydopamine/Au nanocomposites, a significantly enhanced photocurrent response was obtained on this photoelectrode, which provides a good and reliable signal for early detection of AD. Under the optimized conditions, the PEC immunosensor displayed a wide linear range from 1 pg/mL to 100 ng/mL and a low detection limit of 0.26 pg/mL. In addition, this PEC immunosensor also presented good selectivity, stability, and reproducibility. This work may provide a promising point-of-care testing method toward advanced PEC immunoassays for AD biomarkers.

Ultrasensitive label-free photoelectrochemical immunosensor for the detection of amyloid β-protein based on Zn:SnO2/SnS2-Au nanocomposites

2020 ◽  
Vol 308 ◽  
pp. 127576 ◽  
Author(s):  
Ning Gao ◽  
Yifeng Zhang ◽  
Keke Gao ◽  
Jiandong Xie ◽  
Lei Liu ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Label Free ◽  
Β Protein

scholarly journals Distinguishing Amyloid β-Protein in a Mouse Model of Alzheimer’s Disease by Label-Free Vibrational Imaging

Biosensors ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 365
Author(s):  
Shaowei Li ◽  
Ziyi Luo ◽  
Renlong Zhang ◽  
Hao Xu ◽  
Ting Zhou ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Mouse Model ◽  
Amyloid Β ◽  
Basic Research ◽  
Amyloid Β Protein ◽  
Label Free ◽  
Model Of Alzheimer’S Disease ◽  
Β Protein ◽  
Anti Stokes

Due to the increase in the average age of humans, Alzheimer’s disease (AD) has become one of the disorders with the highest incidence worldwide. Abnormal amyloid β protein (Aβ) accumulation is believed to be the most common cause of AD. Therefore, distinguishing the lesion areas can provide clues for AD diagnosis. Here, we present an optical spectroscopy and imaging approach based on coherent anti-Stokes Raman scattering (CARS). Label-free vibrational imaging of Aβ in a mouse model of AD was performed to distinguish the lesion areas by studying the spectra of regions with and without Aβ plaques. Raman spectra in Aβ and non-Aβ regions exhibited a specific difference in the intensity ratio of the wave peaks detected at 2850 and 2930 cm–1. In the non-Aβ region, the ratio of the peak intensity at 2850 cm–1 to that at 2930 cm–1 was approximately 1, whereas that in the Aβ region was 0.8. This label-free vibrational imaging may provide a new method for the clinical diagnosis and basic research of AD.

Label-free photoelectrochemical immunosensor for amyloid β-protein detection based on SnO2/CdCO3/CdS synthesized by one-pot method

2019 ◽  
Vol 126 ◽  
pp. 23-29 ◽  
Author(s):  
Yifeng Zhang ◽  
Mengdi Wang ◽  
Yaoguang Wang ◽  
Jinhui Feng ◽  
Yong Zhang ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Protein Detection ◽  
Amyloid Β Protein ◽  
Label Free ◽  
One Pot ◽  
Β Protein

scholarly journals Extracellular Protein Aggregates Colocalization and Neuronal Dystrophy in Comorbid Alzheimer’s and Creutzfeldt–Jakob Disease: A Micromorphological Pilot Study on 20 Brains

2021 ◽  
Vol 22 (4) ◽  
pp. 2099
Author(s):  
Nikol Jankovska ◽  
Tomas Olejar ◽  
Radoslav Matej
Keyword(s):  
Prion Protein ◽  
Fluorescent Microscopy ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Key Characteristics ◽  
Jakob Disease ◽  
Immunohistochemical Methods ◽  
Confocal Fluorescent Microscopy ◽  
Codon 129

Alzheimer’s disease (AD) and sporadic Creutzfeldt–Jakob disease (sCJD) are both characterized by extracellular pathologically conformed aggregates of amyloid proteins—amyloid β-protein (Aβ) and prion protein (PrPSc), respectively. To investigate the potential morphological colocalization of Aβ and PrPSc aggregates, we examined the hippocampal regions (archicortex and neocortex) of 20 subjects with confirmed comorbid AD and sCJD using neurohistopathological analyses, immunohistochemical methods, and confocal fluorescent microscopy. Our data showed that extracellular Aβ and PrPSc aggregates tended to be, in most cases, located separately, and “compound” plaques were relatively rare. We observed PrPSc plaque-like structures in the periphery of the non-compact parts of Aβ plaques, as well as in tau protein-positive dystrophic structures. The AD ABC score according to the NIA-Alzheimer’s association guidelines, and prion protein subtype with codon 129 methionine–valine (M/V) polymorphisms in sCJD, while representing key characteristics of these diseases, did not correlate with the morphology of the Aβ/PrPSc co-aggregates. However, our data showed that PrPSc aggregation could dominate during co-aggregation with non-compact Aβ in the periphery of Aβ plaques.

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