Construction of artificial peroxidase based on myoglobin scaffold for efficient degradation of meloxicam

IF 3.8 2区化学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Journal of Inorganic Biochemistry Pub Date : 2024-09-12 DOI:10.1016/j.jinorgbio.2024.112733

Weikang Zhang , Yadan Yang , Xiangmin Meng , Fang Wang , Ying-Wu Lin , Jiakun Xu

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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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基于肌红蛋白支架构建人工过氧化物酶以高效降解美洛昔康

通过计算机模拟和基因工程技术的结合，开发出了一种新型人工过氧化物酶，用于高效降解非甾体类消炎药美洛昔康。结果表明，人工过氧化物酶能在 90 秒内完全降解美洛昔康，降解率达 100%，远高于天然漆的降解率（46%）。人工酶的反应时间明显短于天然过氧化物酶（10 分钟）和漆酶（48 小时）。进一步的研究表明，蛋白质活性位点的氨基酸排列对催化性能起着重要作用。采用 UPLC-MS 分析方法揭示了美洛昔康的降解途径。体外毒性试验表明，美洛昔康降解后毒性完全消失。因此，该生物催化系统被证明是绿色降解美洛昔康的有效途径，具有重要的应用潜力。

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来源期刊

Journal of Inorganic Biochemistry 生物-生化与分子生物学

CiteScore

7.00

自引率

10.30%

发文量

336

审稿时长

41 days

期刊介绍： The Journal of Inorganic Biochemistry is an established international forum for research in all aspects of Biological Inorganic Chemistry. Original papers of a high scientific level are published in the form of Articles (full length papers), Short Communications, Focused Reviews and Bioinorganic Methods. Topics include: the chemistry, structure and function of metalloenzymes; the interaction of inorganic ions and molecules with proteins and nucleic acids; the synthesis and properties of coordination complexes of biological interest including both structural and functional model systems; the function of metal- containing systems in the regulation of gene expression; the role of metals in medicine; the application of spectroscopic methods to determine the structure of metallobiomolecules; the preparation and characterization of metal-based biomaterials; and related systems. The emphasis of the Journal is on the structure and mechanism of action of metallobiomolecules.