Fluorometric determination of the activity of alkaline phosphatase based on a system composed of WS2 quantum dots and MnO2 nanosheets

Abstract

A fluorometric method is described for the detection of alkaline phosphatase (ALP) activity. It is based on the use of the product of hydrolysis of the drug amifostine (a thiophosphoester) by ALP. It is known that MnO2 nanosheets quench the blue fluorescence of tungsten disulfide quantum dots (WS2 QDs) which have excitation/emission wavelengths of 320/448 nm. However, in the presence of ALP and amifostine, the product of hydrolysis [2-(3-aminopropylamino)ethanethiol] triggers the decomposition of the MnO2 nanosheets. This results in the recovery of fluorescence. Based on this finding, an assay for ALP activity was developed that works in the 0.09–1.6 U L−1 range, with a 40 mU L−1 detection limit. The relative standard deviation is 1.87% for five repeated measurements of 0.8 U L−1 ALP. The method was applied to the analysis of ALP in real samples and gave satifactory results. Graphical abstract Schematic representation of a fluorometric method for determination of the activity of alkaline phosphatase (ALP). The fluorescence of a system composed of WS2 quantum dots and MnO2 nanosheets is quenched. Hydrolysis of the cytoprotective adjuvant amifostine (a phosphothioester) by ALP leads to a thiol that causes the decomposition of the MnO2 nanosheets. As a result, the blue fluorescence of the system becomes increasingly restored. Schematic representation of a fluorometric method for determination of the activity of alkaline phosphatase (ALP). The fluorescence of a system composed of WS2 quantum dots and MnO2 nanosheets is quenched. Hydrolysis of the cytoprotective adjuvant amifostine (a phosphothioester) by ALP leads to a thiol that causes the decomposition of the MnO2 nanosheets. As a result, the blue fluorescence of the system becomes increasingly restored.