Dataset Information

Iron-Coordinated L-Lysine-Based Nanozymes with High Peroxidase-like Activity for Sensitive Hydrogen Peroxide and Glucose Detection.

ABSTRACT: It is crucial to develop sensitive and accurate sensing strategies to detect H₂O₂ and glucose in biological systems. Herein, biocompatible iron-coordinated L-lysine-based hydrogen peroxide (H₂O₂)-mimetic enzymes (Lys-Fe-NPs) were prepared by precipitation polymerization in aqueous solution. The coordinated Fe²⁺ ion acted as centers of peroxidase-like enzymes of Lys-Fe-NPs, and the catalytic activity was evaluated via the oxidation of 3,3',5,5'-tetramethylbenzidine (TMB) by H₂O₂. Therefore, a sensitive colorimetric detection sensor for H₂O₂ was constructed with a linear range of 1 to 200 μM and a detection limit of 0.51 μM. The same method could also be applied to highly sensitive and selective detection of glucose, with a linear range of 0.5 to 150 μM and a detection limit of 0.32 μM. In addition, an agarose-based hydrogel biosensor colorimetric was successfully implemented for visual assessment and quantitative detection of glucose. The design provided a novel platform for constructing stable and nonprotein enzyme mimics with lysine and showed great potential applications in biorelevant assays.

SUBMITTER: Hou X

PROVIDER: S-EPMC10383789 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature

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Iron-Coordinated L-Lysine-Based Nanozymes with High Peroxidase-like Activity for Sensitive Hydrogen Peroxide and Glucose Detection.

Hou Xiuqing X Wang Ruoxue R Zhang Huijuan H Zhang Meng M Qu Xiongwei X Hu Xiuli X

Polymers 20230710 14

It is crucial to develop sensitive and accurate sensing strategies to detect H2O2 and glucose in biological systems. Herein, biocompatible iron-coordinated L-lysine-based hydrogen peroxide (H2O2)-mimetic enzymes (Lys-Fe-NPs) were prepared by precipitation polymerization in aqueous solution. The coordinated Fe2+ ion acted as centers of peroxidase-like enzymes of Lys-Fe-NPs, and the catalytic activity was evaluated via the oxidation of 3,3',5, ...[more]

PMID: 37514392

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Project description:Thiol proteins are important in cellular antioxidant defenses and redox signalling. It is postulated that reactive oxidants cause selective thiol oxidation, but relative sensitivities of different cell proteins and critical targets are not well characterized. We exposed Jurkat cells to H2O2 for 10 min and measured changes in reversibly oxidized proteins by labelling with iodoacetamidofluorescein and two-dimensional electrophoresis. At 200 microM H2O2, which caused activation of the MAP (mitogen-activated protein) kinase ERK (extracellular-signal-regulated kinase), growth arrest and apoptosis, relatively few changes were seen. A total of 28 spots were reversibly oxidized (increased labelling intensity) and 24 decreased. The latter included isoforms of peroxiredoxins 1 and 2, which were irreversibly oxidized. Oxidation of GAPDH (glyceraldehyde-3-phosphate dehydrogenase) was striking, and other affected proteins included glutathione S-transferase P1-1, enolase, a regulatory subunit of protein kinase A, annexin VI, the mitotic checkpoint serine/threonine-protein kinase BUB1beta, HSP90beta (heat-shock protein 90beta) and proteosome components. At 20 microM H2O2, changes were fewer, but GAPDH and peroxiredoxin 2 were still modified. Dinitrochlorobenzene treatment, which inhibited cellular thioredoxin reductase and partially depleted GSH, caused reversible oxidation of several proteins, including thioredoxin 1 and peroxiredoxins 1 and 2. Most changes were distinct from those with H2O2, and changes with H2O2 were scarcely enhanced by dinitrochlorobenzene. Relatively few proteins, including deoxycytidine kinase, nucleoside diphosphate kinase and a proteosome activator subunit, responded only to the combined treatment. Thus most of the effects of H2O2 were not linked to thioredoxin oxidation. Our study has identified peroxiredoxin 2 and GAPDH as two of the most oxidant-sensitive cell proteins and has highlighted how readily peroxiredoxins undergo irreversible oxidation.

Dataset Information

Iron-Coordinated L-Lysine-Based Nanozymes with High Peroxidase-like Activity for Sensitive Hydrogen Peroxide and Glucose Detection.

Publications

Iron-Coordinated L-Lysine-Based Nanozymes with High Peroxidase-like Activity for Sensitive Hydrogen Peroxide and Glucose Detection.

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