期刊
ACS SYNTHETIC BIOLOGY
卷 11, 期 11, 页码 3797-3804出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssynbio.2c00387
关键词
protein-polymer conjugates; artificial enzymes; polymer modularity; L-proline catalysis; asymmetric aldol catalysis
资金
- Independent Research Fund Denmark (DFF) in the framework of the DFF starting grant
- Novo Nordisk Foundation
- China Scholarship Council [201606210135]
This study proposes an advanced artificial enzyme by polymeric modularity as an efficient aldolase mimic for aqueous asymmetric aldol reactions. The tailored conjugates exhibited remarkable catalytic performance and excellent selectivity. Additionally, the artificial enzyme showed high tolerance and reusability.
Artificial enzymes are becoming a powerful toolbox for selective organic syntheses. Herein, we first propose an advanced artificial enzyme by polymeric modularity as an efficient aldolase mimic for aqueous asymmetric aldol reactions. Based on an in-depth understanding of the aldolase reaction mechanism and our previous work, we demonstrate the modular design of protein-polymer conjugates by co-incorporating L-proline and styrene onto a noncatalytic protein scaffold with a high degree of controllability. The tailored conjugates exhibited remarkable catalytic performance toward the aqueous asymmetric aldol reaction of p-nitrobenzaldehyde and cyclohexanone, achieving 94% conversion and excellent selectivity (95/5 diastereoselectivity, 98% enantiomeric excess). In addition, this artificial enzyme showed high tolerance against extreme conditions (e.g., wide pH range, high temperature) and could be reused for more than four times without significant loss of reactivity. Experiments have shown that the artificial enzyme displayed broad specificity for various aldehydes.
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