Colorimetric detection of acetylcholinesterase and its inhibitor based on thiol-regulated oxidase-like activity of 2D palladium square nanoplates on reduced graphene oxide
- PMID: 33839958
- DOI: 10.1007/s00604-021-04817-x
Colorimetric detection of acetylcholinesterase and its inhibitor based on thiol-regulated oxidase-like activity of 2D palladium square nanoplates on reduced graphene oxide
Abstract
A convenient and sensitive colorimetric assay for acetylcholinesterase (AChE) and its inhibitor has been designed based on the oxidase-like activity of {100}-faceted Pd square nanoplates which are grown in situ on reduced graphene oxide (PdSP@rGO). PdSP@rGO can effectively catalyze the oxidation of colorless 3,3',5,5'-tetramethylbenzidine (TMB) without the assistance of H2O2 to generate blue oxidized TMB (oxTMB) with a characteristic absorption peak at 652 nm. In the presence of AChE, acetylthiocholine (ATCh), a typical AChE substrate, is hydrolyzed to thiocholine (TCh). The generated TCh can effectively inhibit the PdSP@rGO-triggered chromogenic reaction of TMB via cheating with Pd, resulting in color fading and decrease in absorbance. Thus, a sensitive probe for AChE activity is constructed with a working range of 0.25-5 mU mL-1 and a limit of detection (LOD) of 0.0625 mU mL-1. Furthermore, because of the inhibition effect of tacrine on AChE, tacrine is also detected through the colorimetric AChE assay system within the concentrations range 0.025-0.4 μM with a LOD of 0.00229 μM. Hence, a rapid and facile colorimetric procedure to sensitively detect AChE and its inhibitor can be anticipated through modulating the oxidase-like activity of PdSP@rGO. Colorimetric method for detection of AChE and its inhibitor is established by modulating the oxidase mimetic activity of {100}-faceted Pd square nanoplates on reduced graphene oxide (PdSP@rGO).
Keywords: Acetylcholinesterase; Biosensors; Colorimetric detection; Oxidase-like activity; Pd square nanoplates; Tacrine determination.
References
-
- Liao S, Han W, Ding H, Xie D, Tan H, Yang S, Wu Z, Shen G, Yu R (2013) Modulated dye retention for the signal-on fluorometric determination of acetylcholinesterase inhibitor. Anal Chem 85(10):4968–4973. https://doi.org/10.1021/ac400865t - DOI - PubMed
-
- Wang M, Gu X, Zhang G, Zhang D, Zhu D (2009) Convenient and continuous fluorometric assay method for acetylcholinesterase and inhibitor screening based on the aggregation-induced emission. Anal Chem 81(11):4444–4449. https://doi.org/10.1021/ac9002722 - DOI - PubMed
-
- Zhang Y, Hei T, Cai Y, Gao Q, Zhang Q (2012) Affinity binding-guided fluorescent nanobiosensor for acetylcholinesterase inhibitors via distance modulation between the fluorophore and metallic nanoparticle. Anal Chem 84(6):2830–2836. https://doi.org/10.1021/ac300436m - DOI - PubMed
-
- Inestrosa NC, Alvarez A, Pérez CA, Moreno RD, Vicente M, Linker C, Casanueva OI, Soto C, Garrido J (1996) Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer’s fibrils: possible role of the peripheral site of the enzyme. Neuron 16(4):881–891. https://doi.org/10.1016/S0896-6273(00)80108-7 - DOI - PubMed
-
- Mousavi MPS, Abd El-Rahman MK, Mahmoud AM, Abdelsalam RM, Bühlmann P (2018) In situ sensing of the neurotransmitter acetylcholine in a dynamic range of 1 nm to 1 mm. ACS Sensors 3(12):2581–2589. https://doi.org/10.1021/acssensors.8b00950 - DOI - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Other Literature Sources
Research Materials