Dual-Enzyme Characteristics of Polyvinylpyrrolidone-Capped Iridium Nanoparticles and Their Cellular Protective Effect against H2O2-Induced Oxidative Damage

材料科学 氧化损伤 氧化磷酸化 纳米颗粒 聚乙烯吡咯烷酮 化学工程 化学 纳米技术 催化作用 生物化学 高分子化学 工程类
作者
Hua Su,Dandan Liu,Meng Zhao,Wei-Liang Hu,Shan‐Shan Xue,Qian Cao,Xue‐Yi Le,Liang‐Nian Ji,Zong‐Wan Mao
出处
期刊:ACS Applied Materials & Interfaces [American Chemical Society]
卷期号:7 (15): 8233-8242 被引量:202
标识
DOI:10.1021/acsami.5b01271
摘要

Polyvinylpyrrolidone-stabilized iridium nanoparticles (PVP-IrNPs), synthesized by the facile alcoholic reduction method using abundantly available PVP as protecting agents, were first reported as enzyme mimics showing intrinsic catalase- and peroxidase-like activities. The preparation procedure was much easier and more importantly, kinetic studies found that the catalytic activity of PVP-IrNPs was comparable to previously reported platinum nanoparticles. Transmission electron microscopy (TEM) and X-ray photoelectron spectroscopy (XPS) characterization indicated that PVP-IrNPs had the average size of approximately 1.5 nm and mainly consisted of Ir(0) chemical state. The mechanism of PVP-IrNPs' dual-enzyme activities was investigated using XPS, Electron spin resonance (ESR) and cytochrome C-based electron transfer methods. The catalase-like activity was related to the formation of oxidized species Ir(0)@IrO2 upon reaction with H2O2. The peroxidase-like activity originated from their ability acting as electron transfer mediators during the catalysis cycle, without the production of hydroxyl radicals. Interestingly, the protective effect of PVP-IrNPs against H2O2-induced cellular oxidative damage was investigated in an A549 lung cancer cell model and PVP-IrNPs displayed excellent biocompatibility and antioxidant activity. Upon pretreatment of cells with PVP-IrNPs, the intracellular reactive oxygen species (ROS) level in response to H2O2 was decreased and the cell viability increased. This work will facilitate studies on the mechanism and biomedical application of nanomaterials-based enzyme mimic.
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