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

IF 3.8 2区 化学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Weikang Zhang , Yadan Yang , Xiangmin Meng , Fang Wang , Ying-Wu Lin , Jiakun Xu
{"title":"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","authors":"Weikang Zhang ,&nbsp;Yadan Yang ,&nbsp;Xiangmin Meng ,&nbsp;Fang Wang ,&nbsp;Ying-Wu Lin ,&nbsp;Jiakun Xu","doi":"10.1016/j.jinorgbio.2024.112733","DOIUrl":null,"url":null,"abstract":"<div><p>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.</p></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":null,"pages":null},"PeriodicalIF":3.8000,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Construction of artificial peroxidase based on myoglobin scaffold for efficient degradation of meloxicam\",\"authors\":\"Weikang Zhang ,&nbsp;Yadan Yang ,&nbsp;Xiangmin Meng ,&nbsp;Fang Wang ,&nbsp;Ying-Wu Lin ,&nbsp;Jiakun Xu\",\"doi\":\"10.1016/j.jinorgbio.2024.112733\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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.</p></div>\",\"PeriodicalId\":364,\"journal\":{\"name\":\"Journal of Inorganic Biochemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":3.8000,\"publicationDate\":\"2024-09-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Inorganic Biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0162013424002575\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Inorganic Biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0162013424002575","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

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。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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

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

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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Journal of Inorganic Biochemistry
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.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信