Artificial Enzymes Combining Proteins with Proline Polymers for Asymmetric Aldol Reactions in Water

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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  • Technische Universität Dresden
  • University of Southern Denmark
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OriginalspracheEnglisch
Seiten (von - bis)4777-4783
Seitenumfang7
FachzeitschriftACS catalysis
Jahrgang12
Ausgabenummer8
PublikationsstatusVeröffentlicht - 15 Apr. 2022
Extern publiziertJa

Abstract

Artificial enzymes, usually created by incorporating one or two abiological catalytic species into protein hosts, are becoming promising tools for biocatalysis. However, they are still far behind natural enzymes due to their limited active sites with low activity and selectivity. Here, we proposed a polymeric approach to generate artificial enzymes by combining proteins with organocatalytic polymers, in which multiple proline organocatalysts are grafted from protein scaffolds via atom-transfer radical polymerization. The resultant artificial polyenzymes, abbreviated as "ArPoly", have similar physicochemical properties as natural enzymes and proved to be effective aldolase mimics for the aqueous asymmetric aldol reaction, in which an optimal ArPoly gave rise to 33% conversion and 94% enantioselectivity. Therefore, we proved the concept of water-soluble proline-based organocatalyst for aqueous asymmetric aldol reactions. This success not only expands the toolbox of asymmetric organocatalysis but also opens other avenues in the field of artificial enzymes where a plethora of proteins/enzymes can be combined with various well-designed organocatalytic polymers for synthetically useful reactions.

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Artificial Enzymes Combining Proteins with Proline Polymers for Asymmetric Aldol Reactions in Water. / Zhang, Ningning; Sun, Zhiyong; Wu, Changzhu.
in: ACS catalysis, Jahrgang 12, Nr. 8, 15.04.2022, S. 4777-4783.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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N1 - Funding Information: We thank the financial support from the Independent Research Fund Denmark (DFF) in the framework of the Sapere Aude leader program. We also thank Novo Nordisk Foundation for its generous funding. We thank Prof. Dr. Marion B. Ansorge-Schumacher for fruitful discussions and generous support. Funding Information: We thank the financial support from the Independent Research Fund Denmark (DFF) in the framework of the Sapere Aude leader program. We also thank Novo Nordisk Foundation for its generous funding. We thank Prof. Dr. Marion B. Ansorge-Schumacher for fruitful discussions and generous support. Publisher Copyright: © 2022 American Chemical Society. All rights reserved.

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