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In vivo guiding nitrogen-doped carbon nanozyme for tumor catalytic therapy.


ABSTRACT: Nanomaterials with intrinsic enzyme-like activities (nanozymes), have been widely used as artificial enzymes in biomedicine. However, how to control their in vivo performance in a target cell is still challenging. Here we report a strategy to coordinate nanozymes to target tumor cells and selectively perform their activity to destruct tumors. We develop a nanozyme using nitrogen-doped porous carbon nanospheres which possess four enzyme-like activities (oxidase, peroxidase, catalase and superoxide dismutase) responsible for reactive oxygen species regulation. We then introduce ferritin to guide nitrogen-doped porous carbon nanospheres into lysosomes and boost reactive oxygen species generation in a tumor-specific manner, resulting in significant tumor regression in human tumor xenograft mice models. Together, our study provides evidence that nitrogen-doped porous carbon nanospheres are powerful nanozymes capable of regulating intracellular reactive oxygen species, and ferritinylation is a promising strategy to render nanozymes to target tumor cells for in vivo tumor catalytic therapy.

SUBMITTER: Fan K 

PROVIDER: S-EPMC5897348 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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In vivo guiding nitrogen-doped carbon nanozyme for tumor catalytic therapy.

Fan Kelong K   Xi Juqun J   Fan Lei L   Wang Peixia P   Zhu Chunhua C   Tang Yan Y   Xu Xiangdong X   Liang Minmin M   Jiang Bing B   Yan Xiyun X   Gao Lizeng L  

Nature communications 20180412 1


Nanomaterials with intrinsic enzyme-like activities (nanozymes), have been widely used as artificial enzymes in biomedicine. However, how to control their in vivo performance in a target cell is still challenging. Here we report a strategy to coordinate nanozymes to target tumor cells and selectively perform their activity to destruct tumors. We develop a nanozyme using nitrogen-doped porous carbon nanospheres which possess four enzyme-like activities (oxidase, peroxidase, catalase and superoxid  ...[more]

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