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Issue 1, 2014
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Selective and sensitive detection of acetylcholinesterase activity using denatured protein-protected gold nanoclusters as a label-free probe

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Abstract

Based on the fluorescence quenching of novel denatured protein-protected gold nanoclusters, a label-free detection method of acetylcholinesterase (AChE) activity has been developed. Using denatured bovine serum albumin (dBSA), in which 35 cysteine residues can interact polyvalently with Au nanoclusters (AuNCs) as a stabilizing agent, water-soluble and stable fluorescent gold nanoclusters were synthesized. The fluorescence of the AuNCs was quenched by thiocholine that was produced from the AChE hydrolysis of S-acetylthiocholine iodide (ACTI) to detect the AChE activity. The linear range of the method was 0.005–0.15 U mL−1. The limit of detection (LOD) was 0.02 mU mL−1. Other enzymes and metal ions, i.e., GPT, γ-GT, GOx, K+, Ca2+ and Na+, showed minimal interference. Using the fluorescence probe, satisfactory results for the detection of the AChE activity in human serum were obtained.

Graphical abstract: Selective and sensitive detection of acetylcholinesterase activity using denatured protein-protected gold nanoclusters as a label-free probe

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Supplementary files

Article information


Submitted
11 Sep 2013
Accepted
17 Oct 2013
First published
18 Oct 2013

Analyst, 2014,139, 285-289
Article type
Paper

Selective and sensitive detection of acetylcholinesterase activity using denatured protein-protected gold nanoclusters as a label-free probe

H. Li, Y. Guo, L. Xiao and B. Chen, Analyst, 2014, 139, 285
DOI: 10.1039/C3AN01736B

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