Article(id=1321833658428797281, tenantId=1146029695717560320, journalId=1283840372199657495, issueId=1321833616112468138, articleNumber=null, orderNo=null, doi=10.3724/SP.J.1123.2025.06023, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1750435200000, receivedDateStr=2025-06-21, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1793079302651, onlineDateStr=2026-10-27, pubDate=1770480000000, pubDateStr=2026-02-08, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1793079302651, onlineIssueDateStr=2026-10-27, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1793079302651, creator=13701087609, updateTime=1793079302651, updator=13701087609, issue=Issue{id=1321833616112468138, tenantId=1146029695717560320, journalId=1283840372199657495, year='2026', volume='44', issue='2', pageStart='117', pageEnd='222', issueExtLink='null', onlineDate='null', pubDate='1770480000000', pubDateStr='2026-02-08', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=0, createTime=1793079292562, creator='13701087609', updateTime=1793079897369, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext={EN=IssueExt(id=1321836152991101799, tenantId=1146029695717560320, journalId=1283840372199657495, issueId=1321833616112468138, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1321836152991101800, tenantId=1146029695717560320, journalId=1283840372199657495, issueId=1321833616112468138, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null, downloadFileDto=null}, startPage=169, endPage=179, ext={EN=ArticleExt(id=1321833658651095394, articleId=1321833658428797281, tenantId=1146029695717560320, journalId=1283840372199657495, language=EN, title=Research progress on the application of molecularly imprinted nanozymes in the field of biosensing, columnId=1321833577285792627, journalTitle=Chinese Journal of Chromatography, columnName=Review, runingTitle=null, highlight=null, articleAbstract=
Enzymes, as biological catalysts, have garnered significant interest due to their exceptional efficiency and specificity. However, the fragility of natural enzymes under varying temperature and pH conditions significantly restricts their broader utilization. In the past few years, noteworthy advancements have been achieved in creating biomimetic enzyme systems. Scientists have effectively designed artificial enzyme-mimicking systems that exhibit outstanding performance through the integration of various components, including small molecule compounds, deoxyribonucleic acid, and nanomaterials. These systems not only exhibit remarkable catalytic efficiency but also offer considerable benefits, such as adjustable activity, simplicity in modification, and enhanced stability and reusability. Nanomachines, as a new type of enzyme analogues, specifically refer to nanomaterials with enzyme-like catalytic functions. They have played a significant role in the development of biomimetic enzyme systems. Since the first report in 2007 that iron oxide nanoparticles have peroxidase (POD) mimicking activity, hundreds of nanomaterials have been confirmed to have catalytic activities similar to those of natural enzymes such as POD and oxidase (OXD). These novel enzyme analogues not only exhibit a wide range of enzyme-like activities and structural similarity to natural enzymes, but also possess unique nanomaterial characteristics, making their catalytic activities controllable and stable. As effective substitutes for natural enzymes, nanomachines have been widely applied in fields such as biosensing, medical treatment, and environmental remediation. While every cutting-edge technology presents certain limitations, nanozymes are not an exception. They encounter notable challenges, especially concerning substrate selectivity, which is essential for effective targeted catalysis and widespread applicability. To address the aforementioned imitation, researchers have been investigating effective approaches to improve the catalytic selectivity of nanozymes. Primarily, two methods are utilized to achieve selective bioanalysis based on nanozyme catalysis: the first method involves merging nanozymes with biological recognition factors (such as natural enzymes, antibodies, DNA strands, and aptamers), while the second focuses on developing nanozymes that possess intrinsic catalytic specificity through techniques like structure-mimetic design, surface modifications, or molecular imprinting. Incorporating external biological recognition elements can undermine both the stability and cost-effectiveness of nanozymes. Additionally, the methods available for the effective conjugation of nanozymes with biological components are still in their infancy. The creation of structure-mimetic nanozymes tends to be intricate and requires meticulous regulation. In contrast, a straightforward and accessible method for generating substrate recognition sites on nanozymes is the application of molecular imprinting technology (MIT). MIT replicates interactions between enzyme substrates or antibody-antigen pairs to fabricate a cavity that is precisely shaped and sized for a particular template molecule, thus facilitating accurate molecular recognition. Due to its exceptional specificity, stability, and reproducibility, MIT is widely utilized in various fields such as biosensing, medical diagnostics, pharmaceutical assessment, sample preparation, and fluorescent detection. Moreover, the inherent advantages of molecularly imprinted polymers (MIPs), such as their economical nature, exceptional selectivity, remarkable thermochemical resilience, and the removal of the need for biologically derived techniques, have rendered molecular imprinting a feasible strategy for mimicking the roles of natural enzymes. Natural enzymes exhibit substrate specificity primarily due to the three-dimensional structure of their active sites. These active sites are meticulously shaped to ensure a perfect match with the spatial configuration of the intended substrate. Following this concept, molecular imprinting nanoenzymes cleverly integrate molecular imprinting techniques with the properties of nanoenzymes, allowing biomimetic catalysts to retain catalytic selectivity while also demonstrating remarkable substrate specificity. This paper first summarizes the fundamental characteristics of nanozymes, then elaborates on the conventional preparation processes for molecularly imprinted nanozymes, and thoroughly explores the impact of molecular imprinting on the catalytic performance of nanozymes. Through an analysis of typical cases, the latest research advancements in molecularly imprinted nanozymes biosensing field are introduced. Finally, this paper discusses the challenges encountered and future development directions in this area, aiming to provide theoretical references and practical guidance for the application of molecular imprinting and nanozymes in biosensing.
, authors=Xuan ZHANG, Shucheng LIU, Jianming PAN
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酶作为生物催化剂,其核心优势在于高效催化和特异性底物识别,这些特性使其在生物化学过程中发挥着不可替代的作用。近年来,仿生酶体系的构建取得了显著的进展,研究者通过整合小分子化合物、脱氧核糖核酸及纳米材料等多元组分,成功地开发出具有优异性能的人工仿酶体系。这类体系不仅展现出良好的催化性能,还具有活性可控、易于修饰、稳定性高和可重复使用等显著优势。然而,纳米酶作为仿生酶体系的重要组成部分,虽然具有突出的催化活性,但其底物识别能力仍存在明显不足。为解决这一问题,研究者开发了分子印迹纳米酶,通过将纳米材料的催化性能与分子印迹的特异性识别机制相结合,实现了对目标分子的精准识别和选择性催化。这种新型仿生催化体系不仅解决了传统纳米酶在底物识别能力方面的不足,还展现出广阔的应用前景,为酶工程领域的发展提供了新的思路和方法。本文首先概述了纳米酶的基本特性,随后阐述了分子印迹纳米酶的常规制备工艺,并深入探讨了分子印迹对纳米酶催化性能的影响。通过典型实例分析,重点介绍了分子印迹纳米酶在生物传感领域的最新研究进展。最后,探讨了该领域面临的挑战及未来发展方向,旨在为分子印迹与纳米酶在生物传感中的应用提供理论参考和实践指导。
, authors=张玄, 刘树成, 潘建明
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1江苏大学化学化工学院, 江苏 镇江 212013)])], figs=[ArticleFig(id=1321833661868126598, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=EN, label=Fig.1, caption=
(a) Mechanism of valine, leucine, and isoleucine with the proposed method on imprinted and not imprinted nanozymes[18], (b) Michaelis-Menten curves and (c) Lineweaver-Burk model of the TMB oxidation by different amino acids based molecularly imprinted TiO2[18], (d) molecular electrostatic diagrams of TC and DMAPMA[19], figureFileSmall=8zSMVE8pFr4f/2pNIGUzaQ==, figureFileBig=F3kSOH2zyExvZVZwAQRkHg==, tableContent=null), ArticleFig(id=1321833661939429767, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=CN, label=图1, caption=
(a)缬氨酸、亮氨酸和异亮氨酸与所构建传感器在印迹型和非印迹型纳米酶中的作用机制[18],不同氨基酸基分子印迹TiO2氧化TMB的(b)Michaelis-Menten曲线和(c)Lineweaver-Burk曲线[18],(d) TC和DMAPMA分子静电图[19]TMB: 3,3′,5,5′-tetramethylbenzidine; TC: tetracycline; DMAPMA: N-[3-(dimethylamino)propyl]methacrylamide. Valine, leucine, and isoleucine served as templates for molecularly imprinted titanium dioxide (MI TiO₂) coated on Ce[Fe(CN)₆]-derived Fe-CeO₂ (denoted as Fe-CeO₂/ValITiO₂, Fe-CeO₂/LeuITiO₂, and Fe-CeO₂/IleITiO₂, respectively.
, figureFileSmall=8zSMVE8pFr4f/2pNIGUzaQ==, figureFileBig=F3kSOH2zyExvZVZwAQRkHg==, tableContent=null), ArticleFig(id=1321833662140756360, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=EN, label=Fig.2, caption=
Schematic illustration of TC detection with Mn-PBANaoH@MIP[19], figureFileSmall=MF9txYtPXOTe2J+y1kQgkA==, figureFileBig=UyP8pWHbJnNRvOZdr9Z+cw==, tableContent=null), ArticleFig(id=1321833662216253833, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=CN, label=图2, caption=
碱蚀刻的分子印迹型锰基普鲁士蓝类似物(Mn-PBANaoH@MIP)用于TC检测的示意图[19], figureFileSmall=MF9txYtPXOTe2J+y1kQgkA==, figureFileBig=UyP8pWHbJnNRvOZdr9Z+cw==, tableContent=null), ArticleFig(id=1321833662291751306, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=EN, label=Fig.3, caption=
Schematic illustration for the fabrication process and operational principle of the electrochemical sensor for S. aureus detection[39], figureFileSmall=w2p5WOObCsyCD68oAaYMgg==, figureFileBig=adi4+y5ib3KJpbaBTfExUg==, tableContent=null), ArticleFig(id=1321833662396608907, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=CN, label=图3, caption=
用于S. aureus检测的电化学传感器构建和工作原理示意图[39]GCE: glassy carbon electrode; CTAB: cetyltrimethylammonium bromide; HAc: acetic acid; BIP: bacteria-imprinted polymer; o-PD: o-phenylenediamine; o-PDox: o-phenylenediamine oxide; H₂O₂: hydrogen peroxide; Van: vancomycin; BSA: bovine serum albumin; DPV: differential pulse voltammetry.
, figureFileSmall=w2p5WOObCsyCD68oAaYMgg==, figureFileBig=adi4+y5ib3KJpbaBTfExUg==, tableContent=null), ArticleFig(id=1321833662480494988, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=EN, label=Fig.4, caption=
Strategy of the fluorescence (Model Ⅰ) and photoelectrochemical (Model Ⅱ) sensing platform for detecting dibutyl phthalate[40], figureFileSmall=Eo9tPgSXT2BFpk87rwm2Hg==, figureFileBig=Wj9ieTFclarIwNRfiIhnxA==, tableContent=null), ArticleFig(id=1321833662585352589, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=CN, label=图4, caption=
用于检测邻苯二甲酸二丁酯的荧光(模型Ⅰ)和光电化学(模型Ⅱ)传感平台的策略[40]APTES: 3-aminopropyltriethoxysilane; TEPS: phenyltriethoxysilane; TEOS: tetramethyl orthosilicate; DBP: dibutyl phthalate; B-CD: carbon dot-embedded DBP; Apt: aptamer; FL: fluorescence; PEC: photoelectrochemical; CTAB@MAPbI3: cetyltrimethylammonium bromide-modified methylammonium lead iodide perovskite; ITO: indium tin oxide.
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Kinetics parameters of Fe3O4, Fe3O4-Lys-Cu and Fe3O4-Lys-Cu@MIP[20]
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| Kinetic parameter | Fe3O4 | Fe3O4-Lys-Cu | Fe3O4-Lys-Cu@MIP | With pre-concentration Fe3O4-Lys-Cu@MIP |
|---|
| vmax/(mmol/min) | 0.39 | 0.52 | 0.55 | 0.68 |
| Km/(mmol/L) | 1.50 | 1.60 | 1.25 | 0.06 |
| vmax/Km | 0.26 | 0.325 | 0.44 | 11.33 |
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Fe3O4、Fe3O4-Lys-Cu以及Fe3O4-Lys-Cu@MIP的动力学参数[20]
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| Kinetic parameter | Fe3O4 | Fe3O4-Lys-Cu | Fe3O4-Lys-Cu@MIP | With pre-concentration Fe3O4-Lys-Cu@MIP |
|---|
| vmax/(mmol/min) | 0.39 | 0.52 | 0.55 | 0.68 |
| Km/(mmol/L) | 1.50 | 1.60 | 1.25 | 0.06 |
| vmax/Km | 0.26 | 0.325 | 0.44 | 11.33 |
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Molecular imprinting nanozyme-based biosensing for analyte detection
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| Material | Methods | Analyte | Linear ranges | LODs | Ref. |
|---|
| AuNP/Co3O4@Mg/Al cLDH | enzyme-linked immunosorbent assay | saxitoxin | 0-1000 ng/mL | 3.17 ng/mL | [23] |
| MIP/Mn-CeO2 | electrochemical | deoxynivalenol | 0.01-50 ng/mL | 0.003 ng/mL | [24] |
| MIL-101(Fe)-NH2@MIP | ratiometric fluorescent, colorimetric | chloramphenicol | 0.5-10 μmol/L, 10-100 μmol/L | 0.84 μmol/L, 1.47 μmol/L | [25] |
| DSMIP@Mn3O4 | colorimetric, electrochemical | tetracycline | 0.5-150 μmol/L, 0.01-20 μmol/L | 0.1 μmol/L, 5 nmol/L | [16] |
| Fe3O4@MIP | colorimetric | tetracycline | 2-225 μmol/L | 0.4 μmol/L | [26] |
| CeO2@PDA@AuNCs-MIPs | fluorescent | methyl paraoxon | 0.45-125 nmol/L | 0.15 nmol/L | [27] |
| MIP/Mn@NC | electrochemiluminescence,colorimetric | phoxim | 0.05-5000 ng/mL, 5-1000 ng/mL | 0.011 ng/mL, 1.27 ng/mL | [28] |
| MTi-MIP | colorimetric | glycoproteins | 10-130 µg/mL | 0.052 μg/mL | [29] |
| Fe-MOF@CMIP | fluorescence | triclocarban | 10 pmol/L-3.5 nmol/L | 8.5 pmol/L | [30] |
| CeO2HNPs@GOx-MIPs | cascade enzyme system | β-D-glucose | 1.2 μmol/L-0.8 mmol/L | 1.0 μmol/L | [31] |
| Fe3O4@Au-GOx-MIPs | electrochemical | β-D-glucose | 10.0 μmol/L-5.0 mmol/L | 5.0 μmol/L | [32] |
| MIP-aptamer-Fe3O4 NP | colorimetric | thrombin | 108.1 pmol/L-2.7×10-5 mol/L | 27.8 pmol/L | [33] |
| MIL-101(Co,Fe) | ratiometric fluorescence, colorimetric | vanillin | 0.5-55 μmol/L, 1-50 μmol/L | 104 nmol/L, 198 nmol/L | [34] |
), ArticleFig(id=1321833662895731089, tenantId=1146029695717560320, journalId=1283840372199657495, articleId=1321833658428797281, language=CN, label=表2, caption=
基于分子印迹纳米酶生物传感用于分析物检测
, figureFileSmall=null, figureFileBig=null, tableContent=
| Material | Methods | Analyte | Linear ranges | LODs | Ref. |
|---|
| AuNP/Co3O4@Mg/Al cLDH | enzyme-linked immunosorbent assay | saxitoxin | 0-1000 ng/mL | 3.17 ng/mL | [23] |
| MIP/Mn-CeO2 | electrochemical | deoxynivalenol | 0.01-50 ng/mL | 0.003 ng/mL | [24] |
| MIL-101(Fe)-NH2@MIP | ratiometric fluorescent, colorimetric | chloramphenicol | 0.5-10 μmol/L, 10-100 μmol/L | 0.84 μmol/L, 1.47 μmol/L | [25] |
| DSMIP@Mn3O4 | colorimetric, electrochemical | tetracycline | 0.5-150 μmol/L, 0.01-20 μmol/L | 0.1 μmol/L, 5 nmol/L | [16] |
| Fe3O4@MIP | colorimetric | tetracycline | 2-225 μmol/L | 0.4 μmol/L | [26] |
| CeO2@PDA@AuNCs-MIPs | fluorescent | methyl paraoxon | 0.45-125 nmol/L | 0.15 nmol/L | [27] |
| MIP/Mn@NC | electrochemiluminescence,colorimetric | phoxim | 0.05-5000 ng/mL, 5-1000 ng/mL | 0.011 ng/mL, 1.27 ng/mL | [28] |
| MTi-MIP | colorimetric | glycoproteins | 10-130 µg/mL | 0.052 μg/mL | [29] |
| Fe-MOF@CMIP | fluorescence | triclocarban | 10 pmol/L-3.5 nmol/L | 8.5 pmol/L | [30] |
| CeO2HNPs@GOx-MIPs | cascade enzyme system | β-D-glucose | 1.2 μmol/L-0.8 mmol/L | 1.0 μmol/L | [31] |
| Fe3O4@Au-GOx-MIPs | electrochemical | β-D-glucose | 10.0 μmol/L-5.0 mmol/L | 5.0 μmol/L | [32] |
| MIP-aptamer-Fe3O4 NP | colorimetric | thrombin | 108.1 pmol/L-2.7×10-5 mol/L | 27.8 pmol/L | [33] |
| MIL-101(Co,Fe) | ratiometric fluorescence, colorimetric | vanillin | 0.5-55 μmol/L, 1-50 μmol/L | 104 nmol/L, 198 nmol/L | [34] |
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