Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide
Amyloid-β peptide (Aβ) is believed to be an important biomarker for the early diagnosis of Alzheimer’s disease. Therefore, practical and reliable methods to assay Aβ levels have been coveted. In this study, a rapid, sensitive, and selective electrochemical method for Aβ(1–40) detection using Cu2+ re...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2015-12-01
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| Series: | Sensing and Bio-Sensing Research |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2214180415300167 |
| _version_ | 1819267124660535296 |
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| author | Satoshi Fujii Daiki Sono Kaoru Matsubara Hitoshi Abe |
| author_facet | Satoshi Fujii Daiki Sono Kaoru Matsubara Hitoshi Abe |
| author_sort | Satoshi Fujii |
| collection | DOAJ |
| description | Amyloid-β peptide (Aβ) is believed to be an important biomarker for the early diagnosis of Alzheimer’s disease. Therefore, practical and reliable methods to assay Aβ levels have been coveted. In this study, a rapid, sensitive, and selective electrochemical method for Aβ(1–40) detection using Cu2+ redox cycling on peptide-modified gold electrodes was developed. A 19-residue peptide that can promote Aβ fibrillization (AFPP) was immobilized onto a gold electrode. After incubating an Aβ solution with the modified electrode for 1 h, a Cu2+ solution was added and cyclic voltammetry measurements were conducted. The voltammetric response was found to be proportional to the Aβ(1–40) concentration in the 0.1–5 μM range, and a detection limit of 18 nM was achieved. Washing with sodium hydroxide and ethylenediaminetetraacetate solutions easily reinitialized the modified electrode. Results obtained using the reinitialized electrode showed good reproducibility. Furthermore, when another amyloidogenic and Cu2+-binding protein amylin was used as the target, no voltammetric response was observed. These results indicate that the AFPP-modified electrode provides a promising, label-free, sensitive, selective, cost-effective, and easy method for the quantification of Aβ. Keywords: Amyloid-β, Alzheimer’s disease (AD), Fibrillization, Electrochemical detection, Nanobiochip, Cu redox |
| first_indexed | 2024-12-23T21:12:11Z |
| format | Article |
| id | doaj.art-c5cef34a3ef14df795b23d12c1286f5a |
| institution | Directory Open Access Journal |
| issn | 2214-1804 |
| language | English |
| last_indexed | 2024-12-23T21:12:11Z |
| publishDate | 2015-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Sensing and Bio-Sensing Research |
| spelling | doaj.art-c5cef34a3ef14df795b23d12c1286f5a2022-12-21T17:31:01ZengElsevierSensing and Bio-Sensing Research2214-18042015-12-016712Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptideSatoshi Fujii0Daiki Sono1Kaoru Matsubara2Hitoshi Abe3Department of Nanobiochemistry, FIRST (Frontiers of Innovative Research in Science and Technology), Konan University, 7-1-20 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan; Corresponding author.Department of Nanobiochemistry, FIRST (Frontiers of Innovative Research in Science and Technology), Konan University, 7-1-20 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, JapanDepartment of Nanobiochemistry, FIRST (Frontiers of Innovative Research in Science and Technology), Konan University, 7-1-20 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, JapanDepartment of Chemistry, Faculty of Science and Technology, Konan University, 8-9-1 Okamoto, Higashinada-ku, Kobe, Hyogo 658-8501, JapanAmyloid-β peptide (Aβ) is believed to be an important biomarker for the early diagnosis of Alzheimer’s disease. Therefore, practical and reliable methods to assay Aβ levels have been coveted. In this study, a rapid, sensitive, and selective electrochemical method for Aβ(1–40) detection using Cu2+ redox cycling on peptide-modified gold electrodes was developed. A 19-residue peptide that can promote Aβ fibrillization (AFPP) was immobilized onto a gold electrode. After incubating an Aβ solution with the modified electrode for 1 h, a Cu2+ solution was added and cyclic voltammetry measurements were conducted. The voltammetric response was found to be proportional to the Aβ(1–40) concentration in the 0.1–5 μM range, and a detection limit of 18 nM was achieved. Washing with sodium hydroxide and ethylenediaminetetraacetate solutions easily reinitialized the modified electrode. Results obtained using the reinitialized electrode showed good reproducibility. Furthermore, when another amyloidogenic and Cu2+-binding protein amylin was used as the target, no voltammetric response was observed. These results indicate that the AFPP-modified electrode provides a promising, label-free, sensitive, selective, cost-effective, and easy method for the quantification of Aβ. Keywords: Amyloid-β, Alzheimer’s disease (AD), Fibrillization, Electrochemical detection, Nanobiochip, Cu redoxhttp://www.sciencedirect.com/science/article/pii/S2214180415300167 |
| spellingShingle | Satoshi Fujii Daiki Sono Kaoru Matsubara Hitoshi Abe Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide Sensing and Bio-Sensing Research |
| title | Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide |
| title_full | Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide |
| title_fullStr | Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide |
| title_full_unstemmed | Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide |
| title_short | Electrochemical quantification of the Alzheimer’s disease amyloid-β (1–40) using amyloid-β fibrillization promoting peptide |
| title_sort | electrochemical quantification of the alzheimer s disease amyloid β 1 40 using amyloid β fibrillization promoting peptide |
| url | http://www.sciencedirect.com/science/article/pii/S2214180415300167 |
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