Defective PtRuTe As Nanozyme with Selectively Enhanced Peroxidase-like Activity

被引:25
|
作者
Shang, Changshuai [1 ,2 ]
Wang, Qingqing [3 ]
Tan, Hao [1 ]
Lu, Shiyu [1 ]
Wang, Shuguang [1 ]
Zhang, Qinghua [4 ]
Gu, Lin [4 ]
Li, Jing [2 ]
Wang, Erkang [2 ]
Guo, Shaojun [1 ]
机构
[1] Peking Univ, Sch Mat Sci & Engn, Beijing 100871, Peoples R China
[2] Chinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Electroanalyt Chem, Changchun 130022, Peoples R China
[3] Harbin Engn Univ, Coll Mat Sci & Chem Engn, Minist Educ, Key Lab Superlight Mat & Surface Technol, Harbin 150001, Peoples R China
[4] Chinese Acad Sci, Inst Phys, Beijing Natl Lab Condensed Matter Phys, Beijing 100190, Peoples R China
来源
JACS AU | 2022年 / 2卷 / 11期
基金
中国博士后科学基金; 中国国家自然科学基金; 北京市自然科学基金; 国家重点研发计划;
关键词
defect; amorphous; noble metal; peroxidase nanozyme; specificity; NANOMATERIALS; PLATINUM;
D O I
10.1021/jacsau.2c00495
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Noble metal based nanozymes show great potential in replacing natural enzymes; however, their development is greatly restricted by their relatively low specificity and activity. Herein, we report the synthesis of a class of amorphous/crystalline PtRuTe nanomaterials with a Pt/Te-enriched core and a Ru-enriched shell as efficient peroxidase mimics with selectively enhanced perox-idase-like activity and suppressed oxidase-like activity. We demonstrate that amorphous domains play a critical role in tuning and optimizing the catalytic properties. The PtRuTe nanozyme with high-percentage defects exhibits superior catalytic activities and kinetics, and the suppressed oxidase-like activity could diminish the interference of O2 in the glucose colorimetric assay. The high catalytic performance can be caused by amorphous phase induced electron redistribution and electronic interactions between different elements and the synergistic effect of multimetallic nanocrystals. The concurrent extraordinary peroxidase-like activity and suppressed oxidase-like activity guarantee the amorphous/crystalline PtRuTe nanozymes as promising alternatives of natural enzymes for biosensing and beyond.
引用
收藏
页码:2453 / 2459
页数:7
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