Atomic-scale strain engineering of atomically resolved Pt clusters transcending natural enzymes

Ke Chen, Guo Li, Xiaoqun Gong, Qinjuan Ren, Junying Wang, Shuang Zhao, Ling Liu, Yuxing Yan, Qingshan Liu, Yang Cao, Yaoyao Ren, Qiong Qin, Qi Xin, Shu-Lin Liu, Peiyu Yao, Bo Zhang, Jingkai Yang, Ruoli Zhao, Yuan Li, Ran Luo, Yikai Fu, Yonghui Li, Wei Long, Shu Zhang, Haitao Dai, Changlong Liu, Jianning Zhang, Jin Chang, Xiaoyu Mu () and Xiao-Dong Zhang ()
Additional contact information
Ke Chen: Tianjin University
Guo Li: Tianjin University
Xiaoqun Gong: Tianjin University
Qinjuan Ren: Tianjin University
Junying Wang: University of North Carolina at Chapel Hill
Shuang Zhao: Tianjin University
Ling Liu: Tianjin University
Yuxing Yan: Tianjin University
Qingshan Liu: Tianjin University
Yang Cao: Tianjin University
Yaoyao Ren: Tianjin Medical University General Hospital
Qiong Qin: Tianjin Medical University General Hospital
Qi Xin: Tianjin University
Shu-Lin Liu: Nankai University
Peiyu Yao: Nankai University
Bo Zhang: Southern University of Science and Technology
Jingkai Yang: Southern University of Science and Technology
Ruoli Zhao: Tianjin University
Yuan Li: Tianjin University
Ran Luo: Tianjin University
Yikai Fu: Tianjin University
Yonghui Li: Tianjin University
Wei Long: Institute of Radiation Medicine Chinese Academy of Medical, Sciences and Peking Union Medical College
Shu Zhang: Tianjin Medical University General Hospital
Haitao Dai: Tianjin University
Changlong Liu: Tianjin University
Jianning Zhang: Tianjin Medical University General Hospital
Jin Chang: Tianjin University
Xiaoyu Mu: Tianjin University
Xiao-Dong Zhang: Tianjin University

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Strain engineering plays an important role in tuning electronic structure and improving catalytic capability of biocatalyst, but it is still challenging to modify the atomic-scale strain for specific enzyme-like reactions. Here, we systematically design Pt single atom (Pt1), several Pt atoms (Ptn) and atomically-resolved Pt clusters (Ptc) on PdAu biocatalysts to investigate the correlation between atomic strain and enzyme-like catalytic activity by experimental technology and in-depth Density Functional Theory calculations. It is found that Ptc on PdAu (Ptc-PA) with reasonable atomic strain upshifts the d-band center and exposes high potential surface, indicating the sufficient active sites to achieve superior biocatalytic performances. Besides, the Pd shell and Au core serve as storage layers providing abundant energetic charge carriers. The Ptc-PA exhibits a prominent peroxidase (POD)-like activity with the catalytic efficiency (Kcat/Km) of 1.50 × 109 mM−1 min−1, about four orders of magnitude higher than natural horseradish peroxidase (HRP), while catalase (CAT)-like and superoxide dismutase (SOD)-like activities of Ptc-PA are also comparable to those of natural enzymes. Biological experiments demonstrate that the detection limit of the Ptc-PA-based catalytic detection system exceeds that of visual inspection by 132-fold in clinical cancer diagnosis. Besides, Ptc-PA can reduce multi-organ acute inflammatory damage and mitigate oxidative stress disorder.

Date: 2024
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DOI: 10.1038/s41467-024-52684-w

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