Nanozymes Inspired by Natural Enzymes

被引:520
作者
Zhang, Ruofei [1 ,2 ]
Yan, Xiyun [1 ,2 ,3 ]
Fan, Kelong [1 ,2 ,3 ]
机构
[1] Chinese Acad Sci, Inst Biophys, Key Lab Prot & Peptide Pharmaceut, CAS Engn Lab Nanozyme, Beijing 100101, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 101408, Peoples R China
[3] Zhengzhou Univ, Nanozyme Med Ctr, Sch Basic Med Sci, Zhengzhou 450052, Peoples R China
来源
ACCOUNTS OF MATERIALS RESEARCH | 2021年 / 2卷 / 07期
基金
中国国家自然科学基金;
关键词
PEROXIDASE CATALYTIC-ACTIVITY; HORSERADISH-PEROXIDASE; COLORIMETRIC DETECTION; OXYGEN REDUCTION; CARBON NANOTUBES; ACTIVE-SITE; SUBSTRATE; HEME; COMPLEXES; BINDING;
D O I
10.1021/accountsmr.1c00074
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
CONSPECTUS: Nanozymes, nanomaterials with enzyme-like activities with high structural stability, adjustable catalytic activity, functional diversity, recyclability, and feasibility in large-scale preparation, have become a hot spot in the field of artificial enzymes in recent years and are expected to become potential surrogates and competitors for natural enzymes in practical applications. With the development of in-depth research and a wide range of application requirements, creating nanozymes with catalytic performance comparable to or even surpassing that of natural enzymes has been the key research topic in this field. Most of the nanozymes reported in the past were obtained based on random synthesis and screening, for which the catalytic efficiency is far inferior to that of natural enzymes. Natural enzymes that have evolved over hundreds of millions of years have developed a lot of high-efficiency catalysis know-how hidden in their structural features. To create highly active nanozymes, we assumed that there is a general structure-activity relationship between nanozymes and natural enzymes and proposed the nanozyme optimization strategy by grafting the catalytic principles of natural enzymes into the rational design of nanozymes. On the basis of this bioinspired strategy, a series of nanozymes that exhibit similar catalytic activities that are closer to or even beyond those of natural enzymes have been successfully synthesized. By now, rationally designed high-activity bioinspired nanozymes have become a hot topic in the current research on nanozymes. In this Account, we focus on recent representative research progress in the systemic design and construction of bioinspired nanozymes and are devoted to introducing strategic concepts in the bioinspired optimization of nanozymes. We show that the de novo design of nanozymes by simulating the amino acid microenvironment and using metal-free architecture and the coordination structure of metal active sites in natural enzymes is an effective strategy for significantly improving the catalytic performance of nanozymes. A future perspective of the challenges and countermeasures of bioinspired nanozymes is proposed on the basis of these achievements. We hope that the biologically inspired perception will arouse widespread interest in fundamental research and practical applications as well as provide inspiration for the rational design of nanozymes.
引用
收藏
页码:534 / 547
页数:14
相关论文
共 75 条
[1]   One-Step Construction of N,P-Codoped Porous Carbon Sheets/CoP Hybrids with Enhanced Lithium and Potassium Storage [J].
Bai, Jing ;
Xi, Baojuan ;
Mao, Hongzhi ;
Lin, Yue ;
Ma, Xiaojian ;
Feng, Jinkui ;
Xiong, Shenglin .
ADVANCED MATERIALS, 2018, 30 (35)
[2]   The catalytic pathway of horseradish peroxidase at high resolution [J].
Berglund, GI ;
Carlsson, GH ;
Smith, AT ;
Szöke, H ;
Henriksen, A ;
Hajdu, J .
NATURE, 2002, 417 (6887) :463-468
[3]   The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket [J].
Bokhove, Marcel ;
Jimenez, Pol Nadal ;
Quax, Wim J. ;
Dijkstra, Bauke W. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (02) :686-691
[4]   New insight into cofactor-free oxygenation from combined experimental and computational approaches [J].
Bui, Soi ;
Steiner, Roberto A. .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2016, 41 :109-118
[5]   Direct Evidence for a Peroxide Intermediate and a Reactive Enzyme-Substrate-Dioxygen Configuration in a Cofactor-free Oxidase [J].
Bui, Soi ;
von Stetten, David ;
Jambrina, Pablo G. ;
Prange, Thierry ;
Colloc'h, Nathalie ;
de Sanctis, Daniele ;
Royant, Antoine ;
Rosta, Edina ;
Steiner, Roberto A. .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2014, 53 (50) :13710-13714
[6]   Bio-inspired nanozyme: a hydratase mimic in a zeolitic imidazolate framework [J].
Chen, Jinxing ;
Huang, Liang ;
Wang, Qingqing ;
Wu, Weiwei ;
Zhang, He ;
Fang, Youxing ;
Dong, Shaojun .
NANOSCALE, 2019, 11 (13) :5960-5966
[7]   Dual Enzyme-like Activities of Iron Oxide Nanoparticles and Their Implication for Diminishing Cytotoxicity [J].
Chen, Zhongwen ;
Yin, Jun-Jie ;
Zhou, Yu-Ting ;
Zhang, Yu ;
Song, Lina ;
Song, Mengjie ;
Hu, Sunling ;
Gu, Ning .
ACS NANO, 2012, 6 (05) :4001-4012
[8]   A heterogeneous single-atom palladium catalyst surpassing homogeneous systems for Suzuki coupling [J].
Chen, Zupeng ;
Vorobyeva, Evgeniya ;
Mitchell, Sharon ;
Fako, Edvin ;
Ortuno, Manuel A. ;
Lopez, Nuria ;
Collins, Sean M. ;
Midgley, Paul A. ;
Richard, Sylvia ;
Vile, Gianvito ;
Perez-Ramirez, Javier .
NATURE NANOTECHNOLOGY, 2018, 13 (08) :702-+
[9]   Helical Carbon Nanotubes: Intrinsic Peroxidase Catalytic Activity and Its Application for Biocatalysis and Biosensing [J].
Cui, Rongjing ;
Han, Zhida ;
Zhu, Jun-Jie .
CHEMISTRY-A EUROPEAN JOURNAL, 2011, 17 (34) :9377-9384
[10]   PROBING STRUCTURE-FUNCTION RELATIONS IN HEME-CONTAINING OXYGENASES AND PEROXIDASES [J].
DAWSON, JH .
SCIENCE, 1988, 240 (4851) :433-439