A sensitive fluorescence biosensor based on metal ion-mediated DNAzyme activity for amplified detection of acetylcholinesterase. Issue 11 (17th May 2022)
- Record Type:
- Journal Article
- Title:
- A sensitive fluorescence biosensor based on metal ion-mediated DNAzyme activity for amplified detection of acetylcholinesterase. Issue 11 (17th May 2022)
- Main Title:
- A sensitive fluorescence biosensor based on metal ion-mediated DNAzyme activity for amplified detection of acetylcholinesterase
- Authors:
- Zhao, Xu-Hua
Dai, Xiao-Chun
Zhou, Ya-Nan
Zhang, Han-Xiao
Cui, Xiao-Hua
Zhai, Xiang
Yu, Bao-Feng
Song, Zhi-Ling - Abstract:
- Abstract : In this paper, we developed an amplified fluorescence biosensor for acetylcholinesterase (AChE) activity detection by taking advantage of the mercury ion-mediated Mgzyme (Mg 2+ -dependent DNAzyme) activity. Abstract : In this paper, we developed an amplified fluorescence biosensor for acetylcholinesterase (AChE) activity detection by taking advantage of the mercury ion-mediated Mgzyme (Mg 2+ -dependent DNAzyme) activity. The catalytic activity of Mgzyme can be inhibited by the formation of T–Hg 2+ –T base pairs between the Mgzyme and mercury ions. Therefore, the Mgzyme–Hg 2+ complex has no activity on a molecular beacon (MB) substrate, which afforded a very weak fluorescence background for this biosensor. After the addition of acetylcholinesterase (AChE), the substrate acetylthiocholine could be hydrolyzed to thiocholine, which has a stronger binding power with mercury ions than T–Hg 2+ –T base pairs. Therefore, the Mgzyme activity was recovered. The activated Mgzyme could hybridize with the MB substrate and undergo many cleavage cycles, resulting in a significant increase of fluorescence intensity. This biosensor displayed high sensitivity with the detection limit as low as 0.01 mU mL −1 . Moreover, this design did not require complex composition and sequence design; thus it is simple and convenient. This biosensor was also applied for the determination of AChE in human blood and showed satisfactory results.
- Is Part Of:
- Analyst. Volume 147:Issue 11(2022)
- Journal:
- Analyst
- Issue:
- Volume 147:Issue 11(2022)
- Issue Display:
- Volume 147, Issue 11 (2022)
- Year:
- 2022
- Volume:
- 147
- Issue:
- 11
- Issue Sort Value:
- 2022-0147-0011-0000
- Page Start:
- 2575
- Page End:
- 2581
- Publication Date:
- 2022-05-17
- Subjects:
- Chemistry, Analytic -- Periodicals
543 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/an?e=1#!issueid=an139020&type=current&issnprint=0003-2654 ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2an00414c ↗
- Languages:
- English
- ISSNs:
- 0003-2654
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0893.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 21731.xml