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Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase
In this paper, we propose a simple colorimetric method for the sensitive and selective detection of alkaline phosphatase (ALP) activity based on the turn off/turn on oxidase mimic activity of His@AuNCs. His@AuNCs/graphene oxide hybrids (His@AuNCs/GO) were easily obtained using the self-assembly meth...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8227771/ https://www.ncbi.nlm.nih.gov/pubmed/34070918 http://dx.doi.org/10.3390/bios11060174 |
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author | Xiao, Fanfan Yu, Yuting Wu, Yang Tian, Lili Zhao, Guoyan Pang, Hailong Du, Jie |
author_facet | Xiao, Fanfan Yu, Yuting Wu, Yang Tian, Lili Zhao, Guoyan Pang, Hailong Du, Jie |
author_sort | Xiao, Fanfan |
collection | PubMed |
description | In this paper, we propose a simple colorimetric method for the sensitive and selective detection of alkaline phosphatase (ALP) activity based on the turn off/turn on oxidase mimic activity of His@AuNCs. His@AuNCs/graphene oxide hybrids (His@AuNCs/GO) were easily obtained using the self-assembly method with poly (diallyldimethylammonium chloride) (PDDA)-coated GO and showed high oxidase-like activity compared with His@AuNCs. We found that the pyrophosphate ion (P(2)O(7)(4−), PPi) could effectively inhibit the oxidase mimic activity of His@AuNCs/GO, and the hydrolysis of PPi by ALP restored the inhibited activity of His@AuNCs/GO, enabling them to efficiently catalyze the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) to generate the blue oxidized product oxTMB. The intensity of the color showed a linear dependency with the ALP activity. ALP was detected in the linear range of 0–40 mU/mL with a low detection limit (LOD) of 0.26 mU/mL (S/N = 3). The proposed method is fast, easy, and can be applied to monitor the ALP activity in serum samples accurately and effectively, which suggests its practicability and reliability in the detection of ALP activity in clinical practice. |
format | Online Article Text |
id | pubmed-8227771 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-82277712021-06-26 Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase Xiao, Fanfan Yu, Yuting Wu, Yang Tian, Lili Zhao, Guoyan Pang, Hailong Du, Jie Biosensors (Basel) Article In this paper, we propose a simple colorimetric method for the sensitive and selective detection of alkaline phosphatase (ALP) activity based on the turn off/turn on oxidase mimic activity of His@AuNCs. His@AuNCs/graphene oxide hybrids (His@AuNCs/GO) were easily obtained using the self-assembly method with poly (diallyldimethylammonium chloride) (PDDA)-coated GO and showed high oxidase-like activity compared with His@AuNCs. We found that the pyrophosphate ion (P(2)O(7)(4−), PPi) could effectively inhibit the oxidase mimic activity of His@AuNCs/GO, and the hydrolysis of PPi by ALP restored the inhibited activity of His@AuNCs/GO, enabling them to efficiently catalyze the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) to generate the blue oxidized product oxTMB. The intensity of the color showed a linear dependency with the ALP activity. ALP was detected in the linear range of 0–40 mU/mL with a low detection limit (LOD) of 0.26 mU/mL (S/N = 3). The proposed method is fast, easy, and can be applied to monitor the ALP activity in serum samples accurately and effectively, which suggests its practicability and reliability in the detection of ALP activity in clinical practice. MDPI 2021-05-30 /pmc/articles/PMC8227771/ /pubmed/34070918 http://dx.doi.org/10.3390/bios11060174 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Xiao, Fanfan Yu, Yuting Wu, Yang Tian, Lili Zhao, Guoyan Pang, Hailong Du, Jie Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase |
title | Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase |
title_full | Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase |
title_fullStr | Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase |
title_full_unstemmed | Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase |
title_short | Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase |
title_sort | restoring the oxidase-like activity of his@auncs for the determination of alkaline phosphatase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8227771/ https://www.ncbi.nlm.nih.gov/pubmed/34070918 http://dx.doi.org/10.3390/bios11060174 |
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