Details
| Original language | English |
|---|---|
| Pages (from-to) | 1892–1899 |
| Number of pages | 8 |
| Journal | Bioconjugate chemistry |
| Volume | 33 |
| Issue number | 10 |
| Early online date | 4 Oct 2022 |
| Publication status | Published - 19 Oct 2022 |
Abstract
Artificial polyenzymes (ArPoly) are tailored combinations of universal protein scaffolds and polymers newly proposed as promising alternatives to natural enzymes to expand the biocatalyst toolbox. The concept of ArPoly has been continuously extended to metal-containing ArPoly to overcome the drawbacks faced by conventional artificial metalloenzymes. Herein, we present a sustainable route to synthesize a novel water-soluble metalloenzyme for copper-catalyzed azide-alkyne cycloadditions in water with remarkable selectivity. In this case, synthetic l-proline monomers were polymerized onto bovine serum albumen in an aqueous medium via copper-mediated "grafting-from"atom-transfer radical polymerization, resulting in protein-polymer-copper conjugates named ArPolyclickase. The copper in ArPolyclickase plays pivotal bifunctional roles, not only as the catalyst for polymerization but also as the coordinated active site for alkyne-azide click catalysis. ArPolyclickase showcases high efficiency, substrate generality, regioselectivity, and ease of product separation for "click chemistry"in water. Notably, ArPolyclickase displays good biocompatibility without imposing copper toxicity on living cells, which offers the prospect for the upcoming bioorthogonal chemistry.
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In: Bioconjugate chemistry, Vol. 33, No. 10, 19.10.2022, p. 1892–1899.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Copper-Containing Artificial Polyenzymes as a Clickase for Bioorthogonal Chemistry
AU - Zhang, Ningning
AU - Bessel, Patrick
AU - Wu, Changzhu
N1 - Funding Information: The authors thank the financial support from the Independent Research Fund Denmark (DFF) within the framework of the Sapere Aude leader program. We are grateful to the Novo Nordisk Foundation for its generous funding. N.Z. thanks the financial support from China Scholarship Council (No. 201606210135). P.B. is grateful for funding from the Hannover School of Nanotechnology (HSN). They thank the Laboratory of Nano and Quantum Engineering (LNQE) for the use of the TEM.
PY - 2022/10/19
Y1 - 2022/10/19
N2 - Artificial polyenzymes (ArPoly) are tailored combinations of universal protein scaffolds and polymers newly proposed as promising alternatives to natural enzymes to expand the biocatalyst toolbox. The concept of ArPoly has been continuously extended to metal-containing ArPoly to overcome the drawbacks faced by conventional artificial metalloenzymes. Herein, we present a sustainable route to synthesize a novel water-soluble metalloenzyme for copper-catalyzed azide-alkyne cycloadditions in water with remarkable selectivity. In this case, synthetic l-proline monomers were polymerized onto bovine serum albumen in an aqueous medium via copper-mediated "grafting-from"atom-transfer radical polymerization, resulting in protein-polymer-copper conjugates named ArPolyclickase. The copper in ArPolyclickase plays pivotal bifunctional roles, not only as the catalyst for polymerization but also as the coordinated active site for alkyne-azide click catalysis. ArPolyclickase showcases high efficiency, substrate generality, regioselectivity, and ease of product separation for "click chemistry"in water. Notably, ArPolyclickase displays good biocompatibility without imposing copper toxicity on living cells, which offers the prospect for the upcoming bioorthogonal chemistry.
AB - Artificial polyenzymes (ArPoly) are tailored combinations of universal protein scaffolds and polymers newly proposed as promising alternatives to natural enzymes to expand the biocatalyst toolbox. The concept of ArPoly has been continuously extended to metal-containing ArPoly to overcome the drawbacks faced by conventional artificial metalloenzymes. Herein, we present a sustainable route to synthesize a novel water-soluble metalloenzyme for copper-catalyzed azide-alkyne cycloadditions in water with remarkable selectivity. In this case, synthetic l-proline monomers were polymerized onto bovine serum albumen in an aqueous medium via copper-mediated "grafting-from"atom-transfer radical polymerization, resulting in protein-polymer-copper conjugates named ArPolyclickase. The copper in ArPolyclickase plays pivotal bifunctional roles, not only as the catalyst for polymerization but also as the coordinated active site for alkyne-azide click catalysis. ArPolyclickase showcases high efficiency, substrate generality, regioselectivity, and ease of product separation for "click chemistry"in water. Notably, ArPolyclickase displays good biocompatibility without imposing copper toxicity on living cells, which offers the prospect for the upcoming bioorthogonal chemistry.
UR - http://www.scopus.com/inward/record.url?scp=85139550587&partnerID=8YFLogxK
U2 - 10.1021/acs.bioconjchem.2c00363
DO - 10.1021/acs.bioconjchem.2c00363
M3 - Article
VL - 33
SP - 1892
EP - 1899
JO - Bioconjugate chemistry
JF - Bioconjugate chemistry
SN - 1043-1802
IS - 10
ER -