Phosphorus Modulated Peroxidase-Like Activity of Carbon Dots for Colorimetric Detection of Acid Phosphatase.

IF 2.2 3区 化学 Q2 INSTRUMENTS & INSTRUMENTATION Applied Spectroscopy Pub Date : 2024-06-01 Epub Date: 2024-03-26 DOI:10.1177/00037028241238246
Yongmei Zhang, Haibo Liang, Xinru Wang, Ying Yu, Yujuan Cao, Manli Guo, Bixia Lin
{"title":"Phosphorus Modulated Peroxidase-Like Activity of Carbon Dots for Colorimetric Detection of Acid Phosphatase.","authors":"Yongmei Zhang, Haibo Liang, Xinru Wang, Ying Yu, Yujuan Cao, Manli Guo, Bixia Lin","doi":"10.1177/00037028241238246","DOIUrl":null,"url":null,"abstract":"<p><p>The precise regulation of nanoenzyme activity is of great significance for application to biosensing analysis. Herein, the peroxidase-like activity of carbon dots was effectively modulated by doping phosphorus, which was successfully employed for sensitive, selective detection of acid phosphatase (ACP). Phosphorus-doped carbon dots (P-CDs) with excellent peroxidase-like activity were synthesized by a one-pot hydrothermal method, and the catalytic activity could be easily modulated by controlling the additional amount of precursor phytic acid. P-CDs could effectively catalyze the oxidation of colorless 3,3',5,5'-tetramethylbenzidine (TMB) to blue TMB oxidation products in the presence of hydrogen peroxide. While ACP was able to catalyze the hydrolysis of L-ascorbyl-2-phosphate trisodium salt (AAP) to produce ascorbic acid (AA), which inhibited the peroxidase-like activity of P-CDs, by combining P-CDs nanoenzymes and ACP-catalyzed hydrolysis the colorimetric method was established for ACP detection. The absorbance variation showed a good linear relationship with ACP concentration in the range of 0.4-4.0 mU/mL with a limit of detection at 0.12 mU/mL. In addition, the method was successfully applied to detect ACP in human serum samples with recoveries in the range of 98.7-101.6%. The work provides an effective strategy for regulating nanoenzymes activity and a low-cost detection technique for ACP.</p>","PeriodicalId":8253,"journal":{"name":"Applied Spectroscopy","volume":" ","pages":"633-643"},"PeriodicalIF":2.2000,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Spectroscopy","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1177/00037028241238246","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/3/26 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"INSTRUMENTS & INSTRUMENTATION","Score":null,"Total":0}
引用次数: 0

Abstract

The precise regulation of nanoenzyme activity is of great significance for application to biosensing analysis. Herein, the peroxidase-like activity of carbon dots was effectively modulated by doping phosphorus, which was successfully employed for sensitive, selective detection of acid phosphatase (ACP). Phosphorus-doped carbon dots (P-CDs) with excellent peroxidase-like activity were synthesized by a one-pot hydrothermal method, and the catalytic activity could be easily modulated by controlling the additional amount of precursor phytic acid. P-CDs could effectively catalyze the oxidation of colorless 3,3',5,5'-tetramethylbenzidine (TMB) to blue TMB oxidation products in the presence of hydrogen peroxide. While ACP was able to catalyze the hydrolysis of L-ascorbyl-2-phosphate trisodium salt (AAP) to produce ascorbic acid (AA), which inhibited the peroxidase-like activity of P-CDs, by combining P-CDs nanoenzymes and ACP-catalyzed hydrolysis the colorimetric method was established for ACP detection. The absorbance variation showed a good linear relationship with ACP concentration in the range of 0.4-4.0 mU/mL with a limit of detection at 0.12 mU/mL. In addition, the method was successfully applied to detect ACP in human serum samples with recoveries in the range of 98.7-101.6%. The work provides an effective strategy for regulating nanoenzymes activity and a low-cost detection technique for ACP.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
用于酸性磷酸酶比色检测的碳点的磷调制过氧化物酶样活性
精确调节纳米酶的活性对于生物传感分析的应用具有重要意义。本文通过掺杂磷有效地调控了碳点的过氧化物酶样活性,并将其成功地应用于酸性磷酸酶(ACP)的灵敏、选择性检测。通过一锅水热法合成了具有优异过氧化物酶样活性的掺磷碳点(P-CDs),并可通过控制前体植酸的添加量轻松调节其催化活性。在过氧化氢存在下,P-CDs 能有效催化无色的 3,3',5,5'-四甲基联苯胺(TMB)氧化成蓝色的 TMB 氧化产物。ACP 能够催化 L-抗坏血酸-2-磷酸三钠盐(AAP)水解生成抗坏血酸(AA),从而抑制 P-CDs 的过氧化物酶样活性。在0.4-4.0 mU/mL范围内,吸光度变化与ACP浓度呈良好的线性关系,检出限为0.12 mU/mL。此外,该方法还成功地用于检测人血清样品中的 ACP,回收率在 98.7-101.6% 之间。该研究为调节纳米酶的活性提供了一种有效的策略,同时也提供了一种低成本的 ACP 检测技术。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
文献相关原料
公司名称
产品信息
麦克林
isopropyl alcohol (IPA)
麦克林
Glutathione (GSH)
阿拉丁
cysteine (Cys)
阿拉丁
tryptophan
阿拉丁
TMB
阿拉丁
Phytic acid (PA)
来源期刊
Applied Spectroscopy
Applied Spectroscopy 工程技术-光谱学
CiteScore
6.60
自引率
5.70%
发文量
139
审稿时长
3.5 months
期刊介绍: Applied Spectroscopy is one of the world''s leading spectroscopy journals, publishing high-quality peer-reviewed articles, both fundamental and applied, covering all aspects of spectroscopy. Established in 1951, the journal is owned by the Society for Applied Spectroscopy and is published monthly. The journal is dedicated to fulfilling the mission of the Society to “…advance and disseminate knowledge and information concerning the art and science of spectroscopy and other allied sciences.”
期刊最新文献
EXPRESS: Convolutional Autoencoder for Automated Pre-Processing of Tumor Cell and Tissue Raman Spectra. EXPRESS: Identification and Quantification of Trace Metal Speciation in Sediments Using Hyperspectral Imaging. Understanding the Role of the Evanescent Field in Attenuated Total Reflection (ATR) Spectroscopy. Quenching-Independent Two-Photon Absorption Laser-Induced Fluorescence Measurements of Atomic Oxygen in High-Enthalpy Air/Carbon Gas-Surface Interaction. Fourier Transform Infrared Microspectroscopy as a Liquid Biopsy Tool to Detect Single Circulating Tumour Cells in the Blood of a Lung Cancer Patient.
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1