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解析碳点纳米酶超氧化物歧化酶活性的催化机制。

Deciphering the catalytic mechanism of superoxide dismutase activity of carbon dot nanozyme.

机构信息

School of Basic Medical Sciences, Xi'an Jiaotong University Health Science Center, Xi'an, Shaanxi, 710061, P. R. China.

CAS Engineering Laboratory for Nanozyme, Key Laboratory of Protein and Peptide Pharmaceutical, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, P. R. China.

出版信息

Nat Commun. 2023 Jan 11;14(1):160. doi: 10.1038/s41467-023-35828-2.

DOI:10.1038/s41467-023-35828-2
PMID:36631476
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9834297/
Abstract

Nanozymes with superoxide dismutase (SOD)-like activity have attracted increasing interest due to their ability to scavenge superoxide anion, the origin of most reactive oxygen species in vivo. However, SOD nanozymes reported thus far have yet to approach the activity of natural enzymes. Here, we report a carbon dot (C-dot) SOD nanozyme with a catalytic activity of over 10,000 U/mg, comparable to that of natural enzymes. Through selected chemical modifications and theoretical calculations, we show that the SOD-like activity of C-dots relies on the hydroxyl and carboxyl groups for binding superoxide anions and the carbonyl groups conjugated with the π-system for electron transfer. Moreover, C-dot SOD nanozymes exhibit intrinsic targeting ability to oxidation-damaged cells and effectively protect neuron cells in the ischemic stroke male mice model. Together, our study sheds light on the structure-activity relationship of C-dot SOD nanozymes, and demonstrates their potential for treating of oxidation stress related diseases.

摘要

具有超氧化物歧化酶(SOD)样活性的纳米酶由于能够清除超氧阴离子而引起了越来越多的关注,超氧阴离子是体内大多数活性氧物种的起源。然而,迄今为止报道的 SOD 纳米酶尚未达到天然酶的活性。在这里,我们报道了一种碳点(C-dot)SOD 纳米酶,其催化活性超过 10,000 U/mg,可与天然酶相媲美。通过选择化学修饰和理论计算,我们表明 C 点的 SOD 样活性依赖于结合超氧阴离子的羟基和羧基以及与π-体系共轭的羰基进行电子转移。此外,C 点 SOD 纳米酶表现出对氧化损伤细胞的固有靶向能力,并有效保护缺血性中风雄性小鼠模型中的神经元细胞。总之,我们的研究阐明了 C 点 SOD 纳米酶的结构-活性关系,并证明了它们在治疗氧化应激相关疾病方面的潜力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/bb8be8de6ff4/41467_2023_35828_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/b84cb4a3ec73/41467_2023_35828_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/79dd1a216f3c/41467_2023_35828_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/ca314629711a/41467_2023_35828_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/ddff1dfd0bcc/41467_2023_35828_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/538a22224fa2/41467_2023_35828_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/77fe10196bee/41467_2023_35828_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/bb8be8de6ff4/41467_2023_35828_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/b84cb4a3ec73/41467_2023_35828_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/79dd1a216f3c/41467_2023_35828_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/ca314629711a/41467_2023_35828_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/ddff1dfd0bcc/41467_2023_35828_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/538a22224fa2/41467_2023_35828_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/77fe10196bee/41467_2023_35828_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f33e/9834297/bb8be8de6ff4/41467_2023_35828_Fig7_HTML.jpg

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