Dataset Information

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

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.

SUBMITTER: Xiao F

PROVIDER: S-EPMC8227771 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature

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

Xiao Fanfan F Yu Yuting Y Wu Yang Y Tian Lili L Zhao Guoyan G Pang Hailong H Du Jie J

Biosensors 20210530 6

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-</ ...[more]

PMID: 34070918

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Project description:BackgroundNecrotizing enterocolitis (NEC) is a devastating disease of intestinal inflammation that primarily affects premature infants. A potential risk factor for necrotizing enterocolitis is exposure of the premature neonatal intestine to environmental bacteria and their proinflammatory products such as lipopolysaccharide. The metalloenzyme alkaline phosphatase (ALP) has been shown to reduce lipopolysaccharide-mediated inflammation. Additionally, premature rat pups have reduced alkaline phosphatase activity and expression as compared to full term pups. To explore the possibility that the human premature neonatal intestine has a paucity of alkaline phosphatase activity, we measured endogenously produced intestinal alkaline phosphatase activity in meconium as a function of gestational age. To test whether breast milk could serve as a source of exogenous alkaline phosphatase to the neonatal intestine through ingestion, we measured alkaline phosphatase activity in breast milk across a range of time points post-birth.MethodsAlkaline phosphatase activity was quantified in 122 meconium samples from infants of gestational ages ranging from 24 to 40 weeks and in 289 breast milk samples collected from 78 individual mothers between days 2-49 post-birth.ResultsWe observed a strong positive correlation between the meconium alkaline phosphatase activity and gestational age, with preterm infants having lower meconium alkaline phosphatase activities than early term or term infants. Breast milk alkaline phosphatase activity was highest in the first week post-birth, with peak alkaline phosphatase activity at day 2 post-birth, followed by relatively low alkaline phosphatase activity in weeks 2-7.ConclusionsOur results are consistent with the two major risk factors for necrotizing enterocolitis development, preterm birth and lack of breast milk feeding, both contributing to a paucity of alkaline phosphatase activity and impaired capacity to detoxify proinflammatory bacterial products such as lipopolysaccharide.

Dataset Information

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

Publications

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

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