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Construction of artificial peroxidase based on myoglobin scaffold for efficient degradation of meloxicam.
Zhang, Weikang; Yang, Yadan; Meng, Xiangmin; Wang, Fang; Lin, Ying-Wu; Xu, Jiakun.
Afiliación
  • Zhang W; State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Laboratory for Marine Drugs and Bioproducts, Qingdao Marine Science and Technology Center, Qingdao 266237, China; College of Marine Science and Biologi
  • Yang Y; State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Laboratory for Marine Drugs and Bioproducts, Qingdao Marine Science and Technology Center, Qingdao 266237, China; College of Marine Science and Biologi
  • Meng X; College of Marine Science and Biological Engineering, Qingdao University of Science and Technology, Qingdao 266042, China. Electronic address: mengxiangmin@qust.edu.cn.
  • Wang F; State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Laboratory for Marine Drugs and Bioproducts, Qingdao Marine Science and Technology Center, Qingdao 266237, China.
  • Lin YW; School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China. Electronic address: ywlin@usc.edu.cn.
  • Xu J; State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Laboratory for Marine Drugs and Bioproducts, Qingdao Marine Science and Technology Center, Qingdao 266237, China. Electronic address: xujk@ysfri.ac.cn.
J Inorg Biochem ; 262: 112733, 2024 Sep 12.
Article en En | MEDLINE | ID: mdl-39293327
ABSTRACT
A novel artificial peroxidase has been developed for the efficient degradation of the non-steroidal anti-inflammatory drug meloxicam by combining computer simulation and genetic engineering techniques. The results showed that the artificial peroxidase was able to completely degrade meloxicam within 90 s, with a degradation rate of 100 %, which was much higher than that of natural lacquer (46 %). The reaction time of the artificial enzyme was significantly shorter than that of natural peroxidase (10 min) and laccase (48 h). Further studies showed that the amino acid arrangement of the active site of the protein plays an important role in the catalytic performance. The degradation pathway of meloxicam was revealed using UPLC-MS analysis. In vitro toxicity assay showed complete disappearance of toxicity after meloxicam degradation. Therefore, the biocatalytic system proved to be an effective route for the green degradation of meloxicam with important application potential.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Inorg Biochem Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Inorg Biochem Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos