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Peroxidase-Mimetic Activity of Feocl Nanosheets for the Colorimetric Determination of Glutathione and Cysteine Publisher Pubmed



Mohammadpour Z1 ; Malekian Jebeli F1 ; Ghasemzadeh S1
Authors
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Authors Affiliations
  1. 1. Biomaterials and Tissue Engineering Department, Breast Cancer Research Center, Motamed Cancer Institute, ACECR, Tehran, 1517964311, Iran

Source: Microchimica Acta Published:2021


Abstract

For the first time the enzyme mimic activity of iron oxychloride (FeOCl) nanosheets has been studied. The intrinsic peroxidase-mimetic activity of the nanosheets in the presence of H2O2 was approved by the efficient oxidation of tetramethylbenzidine (TMB). The Michaelis–Menten constant of the nanosheets toward TMB was about six times lower than that of natural horseradish peroxidase. The superiority of the nanosheets’ catalytic property ascribes to their H2O2 activation ability. Based on the inhibition of the nanozymes’ catalytic reaction, an assay was developed for the quantitative measurement of glutathione (GSH) and cysteine (Cys). The linear range for both biomolecules was over the range of 3–33 μM. The LOD values (3σ/slope) for GSH and Cys were 2.23 μM and 2.76 μM, respectively. Importantly, we succeeded in colorimetric discrimination of GSH and Cys kinetically. We achieved high selectivity toward GSH and Cys. This work extends the feasibility of using FeOCl as nanozymes to construct biosensors, colorimetric probes for medical diagnosis, and nanozyme-based cancer therapy. Graphical abstract: [Figure not available: see fulltext.]. © 2021, The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.