Abstract
Transactive response DNA binding protein (TDP-43) is a biomarker associated with neurodegenerative diseases, specifically amyotrophic lateral sclerosis (ALS). ALS remains without treatment or a cure, and diagnosis relies on the onset of symptoms. Hence, novel methods are needed for the early detection of TDP-43 as an ALS biomarker. Toward this aim, the detection of full-length phosphorylated TDP-43 (pTDP-43) was achieved by using the electrochemical impedance spectroscopy (EIS)-based biosensor. The TDP-43 antibodies (Abs) on gold (Au) surfaces (Ab-Au) were employed as recognition probes for the protein detection. EIS was used to characterize the Ab-Au surface before and after pTDP-43 binding. In the presence of a solution redox probe, [Fe(CN)6]3−/4−, the dramatic changes in the charge-transfer resistance (Rct) values were observed after the pTDP-43 binding and were directly related to the amount of protein present in solution. Sensitivity for pTDP-43 was highly dependent on the antibody used as a recognition probe, and the pTDP-43 was detected at the limit of detection of 11 ± 6 nM with a large dynamic range, and excellent selectivity against the common bovine serum albumin. This study provides the example of a methodology for fabricating an immunosensor as a recognition layer for ALS protein which can be easily extended for the detection of other disease-related biomarkers.
Funder
Canadian Network for Research and Innovation in Machining Technology, Natural Sciences and Engineering Research Council of Canada
Publisher
The Electrochemical Society
Subject
Materials Chemistry,Electrochemistry,Surfaces, Coatings and Films,Condensed Matter Physics,Renewable Energy, Sustainability and the Environment,Electronic, Optical and Magnetic Materials
Cited by
1 articles.
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