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      Oxygen‐Vacancy‐Rich Piezoelectric BiO 2− x Nanosheets for Augmented Piezocatalytic, Sonothermal, and Enzymatic Therapies

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          Abstract

          Piezocatalytic therapy is a new‐emerging reactive oxygen species (ROS)‐enabled therapeutic strategy that relies on built‐in electric field and energy‐band bending of piezoelectric materials activated by ultrasound (US) irradiation. Despite becoming a hot topic, material development and mechanism exploration are still underway. Herein, as‐synthesized oxygen‐vacancy‐rich BiO 2− x nanosheets (NSs) demonstrate outstanding piezoelectric properties. Under US, a piezo‐potential of 0.25 V for BiO 2− x NSs is sufficient to tilt the conduction band to be more negative than the redox potentials of O 2/ O 2 , O 2 /H 2O 2, and H 2O 2/ OH, which initiates a cascade reaction for ROS generation. Moreover, the BiO 2− x NSs exhibit peroxidase and oxidase‐like activities to augment ROS production, especially in the H 2O 2‐overexpressed tumor microenvironment. Density functional theory calculations show that the generated oxygen vacancies in BiO 2− x NSs are favorable for H 2O 2 adsorption and increasing the carrier density to produce ROS. Furthermore, the quick movement of electrons enables an excellent sonothermal effect, for example, rapid rise in temperature to nearly 65 °C upon US with low power (1.2 W cm −2) and short time (96 s). Therefore, this system realizes a multimode synergistic combination of piezocatalytic, enzymatic, and sonothermal therapies, providing a new direction for defect engineering‐optimized piezoelectric materials for tumor therapy.

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          The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology.

          For a long time, superoxide generation by an NADPH oxidase was considered as an oddity only found in professional phagocytes. Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91(phox)), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). Activation mechanisms and tissue distribution of the different members of the family are markedly different. The physiological functions of NOX family enzymes include host defense, posttranlational processing of proteins, cellular signaling, regulation of gene expression, and cell differentiation. NOX enzymes also contribute to a wide range of pathological processes. NOX deficiency may lead to immunosuppresion, lack of otoconogenesis, or hypothyroidism. Increased NOX activity also contributes to a large number or pathologies, in particular cardiovascular diseases and neurodegeneration. This review summarizes the current state of knowledge of the functions of NOX enzymes in physiology and pathology.
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            Nanozymes: Classification, Catalytic Mechanisms, Activity Regulation, and Applications

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              Reactive Oxygen Species (ROS)-Based Nanomedicine

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                Author and article information

                Contributors
                Journal
                Advanced Materials
                Advanced Materials
                Wiley
                0935-9648
                1521-4095
                July 2023
                June 2023
                July 2023
                : 35
                : 29
                Affiliations
                [1 ] Key Laboratory of Superlight Materials and Surface Technology Ministry of Education College of Materials Science and Chemical Engineering Harbin Engineering University Harbin 150001 P. R. China
                [2 ] State Key Laboratory of Rare Resource Utilization Changchun Institute of Applied Chemistry Chinese Academy of Sciences Changchun 130022 P. R. China
                [3 ] Key Laboratory of Functional Inorganic Material Chemistry Ministry of Education School of Chemistry and Materials Science Heilongjiang University Harbin 150080 P. R. China
                Article
                10.1002/adma.202300648
                37058740
                5a0bc33f-1ccc-40f7-9493-ed300f078920
                © 2023

                http://onlinelibrary.wiley.com/termsAndConditions#vor

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