Up to now, the biocatalytic activity of nanozymes has been extensively studied, while little research focus on their inhibitory behaviors. Here, Co-based carbon material (Co-DMOF) containing abundant carboxylic acid groups was prepared, with defects introduced by COx escape during pyrolysis to achieve controllable activity. As a result, Co-DMOF exhibited biocatalytic activity similar to cytochrome P450 3A4 (CYP3A4) in the metabolism of 1,4-Dihydropyridine (1,4-DHP, a calcium channel blocker). Excitingly, studies on IC and drug-drug interaction (DDI) suggested that Co-DMOF had similar inhibitory behaviors to CYP3A4. Moreover, Co-DMOF displayed excellent stability even under high temperature (100 °C), organic solvents, and a wide range of pH (4-9). Additionally, it can be reused for at least 7 times with only slight loss of activity. Therefore, Co-DMOF has great potential to become a low-cost alternative to CYP3A4 for drug dosage guideline, drug metabolism and DDI. This work provides more possibilities for expanding the CYP3A4-like nanozyme library.
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http://dx.doi.org/10.1016/j.bioorg.2024.107882 | DOI Listing |
J Hazard Mater
January 2025
School of Geographical Science, Harbin Normal University, Harbin 150025, China.
Microplastics (MPs) pose an emerging threat to vegetable growing soils in Harbin, which have a relatively high abundance (11,065 n/kg) with 17.26 of potential ecological risk of single polymer hazard (EI) and 33.92 of potential ecological risk index (PERI).
View Article and Find Full Text PDFNat Commun
January 2025
State Key Laboratory of Medicinal Chemical Biology, College of Chemistry, Nankai University, Tianjin, 300071, P.R. China.
Two or more catalysts conducting multistep reactions in the same reactor, concurrent tandem catalysis, could enable (bio)pharmaceutical and fine chemical manufacturing to become much more sustainable. Herein we report that co-immobilization of metal nanoparticles and a biocatalytic system within a synthetic covalent organic framework capsule, COFcap-2, functions like an artificial cell in that, whereas the catalysts are trapped within 300-400 nm cavities, substrates/products can ingress/egress through ca. 2 nm windows.
View Article and Find Full Text PDFCell
January 2025
State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China; Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai 200240, China; Research Center for Proteins & Bits, Lumy Biotechnology, Changzhou, Jiangsu 213200, China. Electronic address:
Biocatalytic cascades with spatial proximity can orchestrate multistep pathways to form metabolic highways, which enhance the overall catalytic efficiency. However, the effect of spatial organization on catalytic activity is poorly understood, and multienzyme architectural engineering with predictable performance remains unrealized. Here, we developed a standardized framework, called iMARS, to rapidly design the optimal multienzyme architecture by integrating high-throughput activity tests and structural analysis.
View Article and Find Full Text PDFBiomacromolecules
January 2025
School of Physics and Astronomy, University of Leeds, Leeds LS2 9JT, U.K.
Enzymes are attractive as catalysts due to their specificity and biocompatibility; however, their use in industrial and biomedical applications is limited by stability. Here, we present a facile approach for enzyme immobilization within "all-enzyme" hydrogels by forming photochemical covalent cross-links between the enzyme glucose oxidase. We demonstrate that the mechanical properties of the enzyme hydrogel can be tuned with enzyme concentration and the data suggests that the dimeric nature of glucose oxidase results in unusual gel formation behavior which suggests a degree of forced induced dimer dissociation and unfolding.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
January 2025
Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland.
A new strategy has been developed to successfully produce the active component danshensu ex vivo. For this purpose, phenylalanine dehydrogenase from Bacillus sphaericus was combined with the novel hydroxyphenylpyruvate reductase from Mentha x piperita, thereby providing an in situ cofactor regeneration throughout the conversion process. The purified enzymes were co-immobilized and subsequently employed in batch biotransformation, resulting in 60% conversion of 10 mM L-dopa within 24 h, with a catalytic amount of NAD as cofactor.
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