Ultrasensitive capacitance sensor to detect amyloid-beta 1-40 in human serum using supramolecular recognition of β-CD/RGO/ITO micro-disk electrode
- Authors
- Le, H.T.N.; Kim, Daesoo; Phan, L.M.T.; Cho, Sungbo
- Issue Date
- 15-Jan-2022
- Publisher
- ELSEVIER
- Keywords
- Alzheimer' s disease; Amyloid beta 1-40 protein; Beta-cyclodextrin; Capacitance biosensor; Non-redox probe; Reduced graphene oxide
- Citation
- Talanta, v.237
- Journal Title
- Talanta
- Volume
- 237
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/82596
- DOI
- 10.1016/j.talanta.2021.122907
- ISSN
- 0039-9140
- Abstract
- In this paper, we developed a new ultrasensitive capacitance sensor for detection of amyloid beta 1-40 (aβ40) protein (one of Alzheimer's disease core biomarkers) in human serum based on the high supramolecular recognition of the β-cyclodextrin/reduced graphene oxide (β-CD/RGO) nanohybrid toward the anti-aβ40 antibody molecule. The sensor was established by immobilizing specific anti-aβ40 antibody onto the β-CD/RGO nanohybrid functionalized on indium tin oxide micro-disk electrode (anti-aβ40/β-CD/RGO/ITO). Detection of aβ40 in the human serum (HS) using the sensor anti-aβ40/β-CD/RGO/ITO is carried out by capacitance measurement without a redox probe to prevent protein denaturation, serving as a convenient strategy for point-of-care diagnosis. In comparison with other studies, the sensor shows a very low limit of detection of 0.69 fg mL−1 in HS, demonstrating its ability for the ultrasensitive detection of aβ40. Using this sensor, the dissociation constant KD of the binding interaction between anti-aβ40 and aβ40 in HS is found to be 2.9 × 10−7 nM, indicating the high binding affinity of antibody–antigen and the suitability of the anti-aβ40/β-CD/RGO/ITO sensor for aβ40 protein detection. The good selectivity of the anti-aβ40/β-CD/RGO/ITO sensor in the presence of differential analytes was also performed in this paper. © 2021 Elsevier B.V.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - IT융합대학 > 전자공학과 > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/82596)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.