Peroxidase-like activity of acetylcholine-based colorimetric detection of acetylcholinesterase activity and an organophosphorus inhibitor

Colorimetric detection of acetylcholinesterase (AChE) and its inhibitor organophosphates (OPs) is attractive for its convenience, but the addition of exogenous catalyst to produce a chromogenic agent may result in complexity and interference. Herein, we first found that acetylcholine (ATCh) itself mimicked peroxidase's activity, based on which a simple and reliable colorimetric system containing ATCh-3,3',5,5'-tetramethylbenzidine (TMB)-H2O2 was developed for the sensitive and selective assay of AChE activity and its inhibitor OPs. Due to the AChE-catalyzed hydrolysis of acetylcholine, the peroxidase-like activity was affected, which was used for highly sensitive detection of AChE activity with a low limit of detection (LOD) of 0.5 mU mL(-1) and a linear detection range from 2.0 to 14 mU mL(-1). Furthermore, due to the inhibition of OPs on AChE, OPs were also detected with the present ATCh regulated colorimetric system with LOD of 4.0 ng mL(-1) and a linear dynamic range from 10 to 10 000 mg L-1. This strategy was also demonstrated to be applicable for pesticide detection in real samples. Meanwhile, the sensing platform can also be implemented on test strips for rapid and visual monitoring of OPs. Thus, this extremely simple colorimetric strategy without the addition of other exogenous catalysts holds great promise for on-site pesticide detection and can be further exploited for sensing applications in the environmental and food safety fields.