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ORIGINAL RESEARCH article

Front. Med. Technol.
Sec. Nano-Based Drug Delivery
Volume 6 - 2024 | doi: 10.3389/fmedt.2024.1493288
This article is part of the Research Topic Nanomaterials and Small Molecule-Enabled Precision Therapeutics, Biosensor and Diagnostics View all articles

Myeloperoxidase Enzyme-Catalyzed Breakdown of Zero-dimension Carbon Quantum dots

Provisionally accepted
  • Department of Biochemical Engineering, Harcourt Butler Technical University, Kanpur, India

The final, formatted version of the article will be published soon.

    Carbon quantum dots (CQDs) have shown considerable interest in multiple fields including bioimaging, biosensing, photocatalysis, ion sensing, heavy metal detection, and therapy due to highly tunable photoluminescence and good photostability. Apart from having optical properties CQDs offer several advantages such as low toxicity, environmental friendliness, affordability, and simple synthesis methods. Furthermore, by modifying their surface and functionality, it's possible to precisely control their physical and chemical characteristics. Nevertheless, the growing utilization of carbon-based nanomaterials (CNMs) requires thorough examination of their potential toxicity and long-term impacts on human health and biological systems. It is very crucial to understand how these carbon quantum dots interact with the innate immune system that plays a vital role in recognizing and clearing foreign particles. Human myeloperoxidase (MPO), a key enzyme highly expressed in neutrophil granulocytes during inflammatory responses, has been shown to facilitate the biodegradation of carbon quantum dots and various carbonbased nanomaterials through oxidative processes. As a member of the peroxidase family, MPO produces hypochlorous acid (HOCl) and a range of reactive intermediates to eliminate pathogens. Consequently, the study of the biodegradability of CQDs within biological systems is essential for accelerating technological advancements. Here, we have assessed breakdown of CQDs through an oxidative process facilitated by a myeloperoxidase (MPO)-based peroxide system. The human MPO enzyme acted as a catalyst for the CQD degradation, and the addition of hydrogen peroxide (H2O2) and sodium chloride (NaCl) was found to accelerate the reaction.

    Keywords: Myeloperoxidase enzyme, Photoluminescence, Hypochlorous Acid, Biodegradation, Peroxidase

    Received: 08 Sep 2024; Accepted: 31 Oct 2024.

    Copyright: © 2024 Singh and Singh. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence:
    Pooja Singh, Department of Biochemical Engineering, Harcourt Butler Technical University, Kanpur, India
    Lalit Kumar Singh, Department of Biochemical Engineering, Harcourt Butler Technical University, Kanpur, India

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.