过氧亚硝酸盐
超氧化物歧化酶
氧化应激
过氧亚硝酸
抗氧化剂
化学
活性氧
生物化学
超氧化物
酶
生物物理学
生物
作者
Fengxian Zhang,Ping Gao,Qi Min,Junjie Hu,Xiao-Zhi Wu,Cao Li,Zechao Zhuang,Zhenpeng Qiu,Ziqiang Xu
出处
期刊:Small
[Wiley]
日期:2025-06-26
标识
DOI:10.1002/smll.202503033
摘要
Abstract Manganese superoxide dismutase (Mn‐SOD) is the most common natural antioxidant enzyme that defends cells against oxidative stress. However, it is intrinsically vulnerable to nitration by peroxynitrite (ONOO − ) to result in accumulation of reactive oxygen species and inducement of acute kidney injury (AKI). Designing Mn‐SOD mimics that are both active and resistant to ONOO − is essential for advancing artificial enzymes and broadening the application of enzymatic catalytic therapies. Herein, an artificial manganese‐based single‐atom nanozymes (Mn‐O 5 /CN SAzyme) featuring square‐pyramidal Mn‐O 5 active sites and abundant hydroxyl groups is presented. Mn‐O 5 /CN SAzyme demonstrates excellent biocompatibility, superior SOD‐like activity, and tolerance to ONOO − , positioning it as a promising artificial enzyme mimics for alleviating AKI. Theoretical calculations suggest that the square‐pyramidal Mn‐O 5 coordination in Mn‐O 5 /CN SAzyme enhances its SOD‐like activity and ONOO − resistance. Mn‐O 5 /CN SAzyme has high antioxidant efficacy toward HK‐2 cells. It significantly reduces renal oxidative stress and inflammation in AKI mice, without any side effects. Mechanistically, Mn‐O 5 /CN SAzyme alleviates AKI by suppressing the pro‐inflammatory cytokine cascade driven by the NOD‐like receptor protein 3 (NLRP3)/caspase‐1/gasdermin D pathway. This study highlights the crucial role of the Mn‐O 5 coordination structure in enhancing SOD‐like activity and ONOO − resistance, presenting a novel strategy for treating inflammatory diseases.
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