دورية أكاديمية
Chimeric Biocatalyst Combining Peptidic and Nucleic Acid Components Overcomes the Performance and Limitations of the Native Horseradish Peroxidase
| العنوان: | Chimeric Biocatalyst Combining Peptidic and Nucleic Acid Components Overcomes the Performance and Limitations of the Native Horseradish Peroxidase |
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| المؤلفون: | Zhang, Xiaobo, Qiu, Dehui, Chen, Jielin, Zhang, Yue, Wang, Jiawei, Chen, Desheng, Liu, Yuan, Cheng, Mingpan, Monchaud, David, Mergny, Jean-Louis, Ju, Huangxian, Zhou, Jun |
| المساهمون: | Nanjing University (NJU), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie Moléculaire de l'Université de Bourgogne Dijon (ICMUB), Université de Bourgogne (UB)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 0002-7863. |
| بيانات النشر: | HAL CCSD American Chemical Society |
| سنة النشر: | 2023 |
| المجموعة: | Université de Bourgogne (UB): HAL |
| مصطلحات موضوعية: | [CHIM.CATA]Chemical Sciences/Catalysis |
| الوصف: | International audience ; Chimeric peptide-DNAzyme (CPDzyme) is a novel design of an artificial peroxidase that relies on the covalent assembly of DNA (quadruplex-DNA, or G4), peptides and an enzyme cofactor (hemin) in a single scaffold. An accurate control of the assembly of these different partners allows for the design of the efficient CPDzyme prototype G4-Hemin-KHRRH, found to be >2,000-fold more active (in terms of conversion number kcat) than the corresponding but non-covalent complex and, more importantly, >1.5-fold active than the corresponding native peroxidase (horseradish peroxidase, or HRP) when considering a single catalytic center. This unique performance originates in a series of improvements gradually made thanks to an accurate selection and arrangement of the different components of the CPDzyme, in order to benefit from synergistic interactions between them. The optimized prototype G4-Hemin-KHRRH is efficient and robust as it can be used under a wide range of non-physiologically relevant conditions (organic solvents, high temperature (95°C), in a wide range of pH (from 2 to 10)), thus compensating for the shortcomings of natural enzymes. Our approach thus opens broad prospects for the design of ever more efficient artificial enzymes. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | hal-03995188; https://hal.science/hal-03995188Test; https://hal.science/hal-03995188/documentTest; https://hal.science/hal-03995188/file/CPDzyme%20-%20personnal%20copy.pdfTest |
| DOI: | 10.1021/jacs.2c11318 |
| الإتاحة: | https://doi.org/10.1021/jacs.2c11318Test https://hal.science/hal-03995188Test https://hal.science/hal-03995188/documentTest https://hal.science/hal-03995188/file/CPDzyme%20-%20personnal%20copy.pdfTest |
| حقوق: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.F03AFA4 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1021/jacs.2c11318 |
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