Second coordination sphere regulates nanozyme inhibition to assist early drug discovery

Early drug discovery is a time- and cost-consuming task requiring enzymes. Although nanozymes with metal sites akin to metallocofactors display similar activities, the lack of proximal amino acids hinders them from more adequately mimicking enzymes for drug discovery purposes. Hence, the rational design of the nanozyme second coordination sphere is desirable yet remains challenging. Herein, we report a nanozyme featuring atomically dispersed Cu-N<sub>4</sub> sites with proximal hydroxyl groups (CuNC-OH). Experimental and theoretical results reveal that Cu-N<sub>4</sub> site and hydroxyl respectively behave as cofactor and amino acid of the enzymatic pocket to interact with adsorbates, regulating nanozyme activity and inhibition. This mechanism involving dual sites is similar to that of thyroid peroxidases, which enables specific inhibition of CuNC-OH by antithyroid drugs. Based on these findings, a nanozyme-assisted drug discovery kit is established to analyze inhibition features of thyroid peroxidase inhibitors and screen out promising antithyroid drugs with a significant cost reduction compared with traditional enzyme kits.

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Publication Details

Journal
Nature Communications
Published
2025-04-01
DOI
https://doi.org/10.1038/s41467-025-58291-7
Citations
13
Primary Topic
Advanced Nanomaterials in Catalysis
Type
article
Field-Weighted Citation Impact
6.73

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article

Second coordination sphere regulates nanozyme inhibition to assist early drug discovery

Weiqing Xu, Chengzhou Zhu, Lirong Zheng, Canglong Wang et al.
13 citations
Nature Communications
Advanced Nanomaterials in Catalysis
6.73
article

Second coordination sphere regulates nanozyme inhibition to assist early drug discovery

Weiqing Xu, Chengzhou Zhu, Lirong Zheng, Canglong Wang, Wenling Gu, Jian Li, Yu Wu, Wenxuan Jiang
article en
13 citations

Abstract

Early drug discovery is a time- and cost-consuming task requiring enzymes. Although nanozymes with metal sites akin to metallocofactors display similar activities, the lack of proximal amino acids hinders them from more adequately mimicking enzymes for drug discovery purposes. Hence, the rational design of the nanozyme second coordination sphere is desirable yet remains challenging. Herein, we report a nanozyme featuring atomically dispersed Cu-N<sub>4</sub> sites with proximal hydroxyl groups (CuNC-OH). Experimental and theoretical results reveal that Cu-N<sub>4</sub> site and hydroxyl respectively behave as cofactor and amino acid of the enzymatic pocket to interact with adsorbates, regulating nanozyme activity and inhibition. This mechanism involving dual sites is similar to that of thyroid peroxidases, which enables specific inhibition of CuNC-OH by antithyroid drugs. Based on these findings, a nanozyme-assisted drug discovery kit is established to analyze inhibition features of thyroid peroxidase inhibitors and screen out promising antithyroid drugs with a significant cost reduction compared with traditional enzyme kits.

Nature CommunicationsVol. 16(1)
European Synchrotron Radiation Facility (FR), Central China Normal University (CN), Ministry of Education (ME), Institute of Modern Physics (CN)
National Natural Science Foundation of China, Central China Normal University, Project 211, Fundamental Research Funds for the Central Universities, Beijing Synchrotron Radiation Facility
Openalex Percentile: Top 3%
Advanced Nanomaterials in Catalysis
6.73
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