Details
| Original language | English |
|---|---|
| Pages (from-to) | 3797-3804 |
| Number of pages | 8 |
| Journal | ACS synthetic biology |
| Volume | 11 |
| Issue number | 11 |
| Publication status | Published - 18 Nov 2022 |
| Externally published | Yes |
Abstract
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.
Keywords
- artificial enzymes, asymmetric aldol catalysis, l -proline catalysis, polymer modularity, protein-polymer conjugates
ASJC Scopus subject areas
- Engineering(all)
- Biomedical Engineering
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry, Genetics and Molecular Biology (miscellaneous)
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In: ACS synthetic biology, Vol. 11, No. 11, 18.11.2022, p. 3797-3804.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Tailoring Protein-Polymer Conjugates as Efficient Artificial Enzymes for Aqueous Asymmetric Aldol Reactions
AU - Zhang, Ningning
AU - Wu, Changzhu
N1 - Funding Information: We are thankful for the financial support from the Independent Research Fund Denmark (DFF) in the framework of the DFF starting grant. Novo Nordisk Foundation is acknowledged for its generous funding. We thank Prof. Marion B. Ansorge-Schumacher for fruitful discussions and generous support. N.Z. is thankfui for the financial support from China Scholarship Council (No. 201606210135). We thank Jian Ning (University of Southern Denmark) for the water contact angle measurement. Publisher Copyright: © 2022 American Chemical Society. All rights reserved.
PY - 2022/11/18
Y1 - 2022/11/18
N2 - 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.
AB - 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.
KW - artificial enzymes
KW - asymmetric aldol catalysis
KW - l -proline catalysis
KW - polymer modularity
KW - protein-polymer conjugates
UR - http://www.scopus.com/inward/record.url?scp=85141678083&partnerID=8YFLogxK
U2 - 10.1021/acssynbio.2c00387
DO - 10.1021/acssynbio.2c00387
M3 - Article
C2 - 36343337
AN - SCOPUS:85141678083
VL - 11
SP - 3797
EP - 3804
JO - ACS synthetic biology
JF - ACS synthetic biology
SN - 2161-5063
IS - 11
ER -