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A bioinspired sulfur–Fe–heme nanozyme with selective peroxidase-like activity for enhanced tumor chemotherapy
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A bioinspired sulfur–Fe–heme nanozyme with selective peroxidase-like activity for enhanced tumor chemotherapy
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Journal Article
A bioinspired sulfur–Fe–heme nanozyme with selective peroxidase-like activity for enhanced tumor chemotherapy
2024
Overview
Iron-based nanozymes, recognized for their biocompatibility and peroxidase-like activities, hold promise as catalysts in tumor therapy. However, their concurrent catalase-like activity undermines therapeutic efficacy by converting hydrogen peroxide in tumor tissues into oxygen, thus diminishing hydroxyl radical production. Addressing this challenge, this study introduces the hemin–cysteine–Fe (HCFe) nanozyme, which exhibits exclusive peroxidase-like activity. Constructed through a supramolecular assembly approach involving Fmoc-
l
-cysteine, heme, and Fe²⁺ coordination, HCFe distinctly incorporates heme and [Fe–S] within its active center. Sulfur coordination to the central Fe atom of Hemin is crucial in modulating the catalytic preference of the HCFe nanozyme towards peroxidase-like activity. This unique mechanism distinguishes HCFe from other bifunctional iron-based nanozymes, enhancing its catalytic selectivity even beyond that of natural peroxidases. This selective activity allows HCFe to significantly elevate ROS production and exert cytotoxic effects, especially against cisplatin-resistant esophageal squamous cell carcinoma (ESCC) cells and their xenografts in female mice when combined with cisplatin. These findings underscore HCFe’s potential as a crucial component in multimodal cancer therapy, notably in augmenting chemotherapy efficacy.
Iron-based nanozymes are promising for tumor catalytic therapy owing to their biocompatibility and peroxidase-like activity, but the concurrent catalase-like activity undermines the therapeutic efficacy. Here, the authors address this issue by developing a hemin–cysteine–Fe nanozyme, which exhibits catalytic selectivity and exclusive peroxidase-like activity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/2
/ 13/31
/ 13/51
/ 14/19
/ 38/91
/ 59
/ Animals
/ Antineoplastic Agents - chemistry
/ Antineoplastic Agents - pharmacology
/ Cancer
/ Catalase
/ Cysteine
/ Female
/ Heme
/ Hemin
/ Humanities and Social Sciences
/ Humans
/ Hydrogen Peroxide - chemistry
/ Hydrogen Peroxide - metabolism
/ Iron
/ Mice
/ Reactive Oxygen Species - metabolism
/ Science
/ Sulfur
/ Tumors
