scholarly journals A Probeless Capacitive Biosensor for Direct Detection of Amyloid Beta 1-42 in Human Serum Based on an Interdigitated Chain-Shaped Electrode

Micromachines ◽  
2020 ◽  
Vol 11 (9) ◽  
pp. 791
Author(s):  
Hien T. Ngoc Le ◽  
Jinsoo Park ◽  
Sungbo Cho

Amyloid beta (aβ) 1-42, a peptide that is 1-42 amino acids long, is a major component of senile plaques in the brains of patients with Alzheimer’s disease. Aβ detection has become an essential antecedence to predict the declining mental abilities of patients. In this paper, a probeless capacitive biosensor for the non-Faradaic detection of aβ 1-42 peptide was developed by immobilizing a specific anti-aβ antibody onto a self-assembled monolayer functionalized interdigitated chain-shaped electrode (anti-aβ/SAM/ICE). The novelty and difference of this article from previous studies is the direct detection of aβ peptide with no redox probe ((Fe(CN)6)3−/4−), which can avoid the denaturation of the protein caused by the metallization (binding of aβ to metal ion Fe which is presented in the redox couple). The direct detection of aβ with no redox probe is performed by non-Faradaic capacitive measurement, which is greatly different from the Faradaic measurement of the charge transfer resistance of the redox probe. The detection of various aβ 1-42 peptide concentrations in human serum (HS) was performed by measuring the relative change in electrode interfacial capacitance due to the specific antibody-aβ binding. Capacitance change in the anti-aβ/SAM/ICE biosensor showed a linear detection range between 10 pg mL−1 and 104 pg mL−1, and a detection limit of 7.5 pg mL−1 in HS, which was much lower than the limit of detection for CSF aβ 1-42 (~500 pg mL−1) and other biosensors. The small dissociation constant Kd of the antibody-antigen interaction was also found to be 0.016 nM in HS, indicating the high binding affinity of the anti-aβ/SAM/ICE biosensor in the recognizing of aβ 1-42. Thus, the developed sensor can be used for label-free and direct measurement of aβ 1-42 peptide and for point-of-care diagnosis of Alzheimer’s disease without redox probe.

2002 ◽  
Vol 38 ◽  
pp. 37-49 ◽  
Author(s):  
Janelle Nunan ◽  
David H Small

The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.


HAPS Educator ◽  
2015 ◽  
Vol 20 (1) ◽  
pp. 38-43
Author(s):  
Brie Paddock ◽  
Kimberly Canfield ◽  
Sarah Cooper

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