| Autor: |
Liu Z; College of Chemistry and Materials Science, Editorial Department of Journal of Anhui Normal University, Anhui Normal University, Wuhu 241000, P. R. China. hywang@mail.ahnu.edu.cn., Wang H; College of Chemistry and Materials Science, Editorial Department of Journal of Anhui Normal University, Anhui Normal University, Wuhu 241000, P. R. China. hywang@mail.ahnu.edu.cn. |
| Jazyk: |
angličtina |
| Zdroj: |
The Analyst [Analyst] 2019 Oct 07; Vol. 144 (19), pp. 5794-5801. Date of Electronic Publication: 2019 Aug 29. |
| DOI: |
10.1039/c9an01430f |
| Abstrakt: |
We report here a highly sensitive sandwich type electrochemical aptasensor for lysozyme (lys) detection by the integration of an antifouling interface with HRP-based signal amplification. The biosensing interface with antifouling ability is designed, consisting of a lys-binding aptamer (LBA), dithiothreitol (DTT) and mercaptohexanol (MCH). When lys is captured by the immobilized LBA due to the specific recognition of the aptamer, gold nanoparticles (AuNPs) functionalized with HRP and LBA (HRP-AuNP-LBA) are further conjugated to the surface-bound lys, forming a sandwich assay format. HRP catalyzes the chemical oxidation of hydroquinone (HQ) by hydrogen peroxide (H 2 O 2 ) to produce benzoquinone (BQ) which results in a large electrochemical reduction signal of BQ. Therefore, this reduction signal measured by differential pulse voltammetry (DPV) is used to detect lys. The catalytic behavior of HRP toward the reaction between HQ and H 2 O 2 , together with the high loading of HRP on AuNPs, remarkably amplifies the signal. A linear relationship between the DPV response and the logarithm of lys concentration from 0.01 pg mL -1 to 10 5 pg mL -1 with a detection limit of 0.003 pg mL -1 (S/N = 3) is obtained. The proposed biosensing platform combines antifouling ability and signal amplification, resulting in high sensitivity, providing an effective way for ultrasensitive assay of protein biomarkers in complex media. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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