Colorimetric assay of acetylcholinesterase inhibitor tacrine based on MoO

Molybdenum dichalcogenides MoX2 (X=S, Se) have been found to possess intrinsic peroxidase-like activity. However, molybdenum oxides (MoO2) as peroxidase mimetics have not been exploited yet. Herein, MoO2 nanoparticles were synthesized by a simple hydrothermal method and found to possess the peroxidase-like activity for the first time. MoO2 nanoparticles could catalyze the oxidation of 3,3',5,5'-tetrametylbenzidine (TMB) by H2O2 to produce a blue-color product (oxTMB). The catalytic property and mechanism were investigated by stead-state kinetics experiment and free radicals scavenging experiment, respectively. Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine chloride (ATCh) into thiocholine (TCh), which could reduce oxTMB to decrease the absorbance in solution. In the presence of AChE inhibitor tacrine, the generation of TCh was inhibited and the absorbance was preserved. Based on these properties, a colorimetric assay method was developed for AChE inhibitor tacrine. This work not only broadens the application of the peroxidase mimetics, but also overcome the disadvantages of traditional methods such as expensive, complex and vulnerable to background interference for colorimetric assay of AChE inhibitor.