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Restoring the Oxidase-Like Activity of His@AuNCs for the Determination of Alkaline Phosphatase

Authors :
Fanfan Xiao
Yuting Yu
Yang Wu
Lili Tian
Guoyan Zhao
Hailong Pang
Jie Du
Source :
Biosensors, Vol 11, Iss 6, p 174 (2021)
Publication Year :
2021
Publisher :
MDPI AG, 2021.

Abstract

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 (P2O74−, 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.

Details

Language :
English
ISSN :
11060174, 20796374, and 41199464
Volume :
11
Issue :
6
Database :
Directory of Open Access Journals
Journal :
Biosensors
Publication Type :
Academic Journal
Accession number :
edsdoj.4119946497844004aea2bcd9d6b5f36d
Document Type :
article
Full Text :
https://doi.org/10.3390/bios11060174