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Gold Nanoparticles Decorated CoAl LDH Monolayer: A Peroxidase-Like Nanozyme for Sensitive Colorimetric Detection of Acetylcholinesterase and Inhibitors.
- Source :
-
Inorganic chemistry [Inorg Chem] 2024 Dec 23; Vol. 63 (51), pp. 24065-24070. Date of Electronic Publication: 2024 Dec 09. - Publication Year :
- 2024
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Abstract
- Monitoring acetylcholinesterase (AChE) activity and its inhibitor is crucial yet challenging for the early diagnosis and treatment of neurological diseases. In this study, we present Au nanoparticle decorated CoAl layered double hydroxide monolayer (Au@CoAl-LDH-m) as a peroxidase-like (POD) nanozyme for the sensitive colorimetric detection of AChE and its inhibitor, thiamine pyrophosphate (TPP). Remarkably, the Au@CoAl-LDH-m nanozyme can catalyze the oxidation of chromogenic substrates through its POD-like activity, which is effectively inhibited by thiocholine (TCh, a catalytic product of AChE), thereby enabling detection of AChE and TPP through a visible colorimetric readout. The approach provides a highly sensitive and specificity assay with a broader linear response range (1-100 mU mL <superscript>-1</superscript> for AChE and 1-1000 ng mL <superscript>-1</superscript> for TPP) and a low detection limit (0.092 mU mL <superscript>-1</superscript> for AChE and 0.201 ng mL <superscript>-1</superscript> for TPP), respectively. These results highlight the significant potential of Au@CoAl-LDH-m for advancing colorimetric sensors in detecting small molecules across various biological applications.
- Subjects :
- Hydroxides chemistry
Peroxidase chemistry
Peroxidase metabolism
Peroxidase antagonists & inhibitors
Limit of Detection
Acetylcholinesterase metabolism
Colorimetry methods
Gold chemistry
Metal Nanoparticles chemistry
Cholinesterase Inhibitors pharmacology
Cholinesterase Inhibitors chemistry
Cholinesterase Inhibitors analysis
Subjects
Details
- Language :
- English
- ISSN :
- 1520-510X
- Volume :
- 63
- Issue :
- 51
- Database :
- MEDLINE
- Journal :
- Inorganic chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 39651768
- Full Text :
- https://doi.org/10.1021/acs.inorgchem.4c04416