Antioxidant activity of Chrysanthemum morifolium Ramat. hydroalcoholic extract and reactivation of acetylcholinesterase enzyme

The acetylcholinesterase (AChE) function is to hydrolyze the acetylcholine (ACh). This enzyme is irreversibly inhibited by the organophosphate compounds of insecticides and nerve gases. This inhibition by the ACh accumulation in the cholinergic synapses leads to the overstimulation and cholinergic crisis in the synaptic cleft. This study was aimed at reactivating the inhibited cholinesterase (ChE) by the Chrysanthemum morifolium Ramat. hydroalcoholic extract. The effects of Ch. morifolium hydroalcoholic extract were evaluated on the activity and ChE reactivation by the Elman staining method. The erythrocyte AChE and plasma butyrylcholinesterase (BChE) were the enzyme sources in this study. The antioxidant activity, identification of functional groups, and determination of compounds in the extract were determined by DPPH, FTIR, and GC/MS methods, respectively. The results showed that the reactivation rate of inhibited BChE (the amount of losing activity in the enzyme inhibited = up to 91.95% ± 0.17) was obtained 49.16% ± 0.24 in the 1 mg.ml-1 of chrysanthemum extract treatment. In this experiment, the AChE enzyme was inhibited up to 30.77% ± 0.45 by paraoxon, which the 1 mg.ml-1 of chrysanthemum extract restored it and eliminated the paraoxon toxicity. The IC50 in the chrysanthemum hydroalcoholic extract for scavenging the DPPH free radicals was calculated 483.67 ± 3 μg.ml-1. The results of FTIR and GC/MS also showed that the extract of this plant is rich in the phenolic compounds containing the hydroxyl and carbonyl groups, which probably play a key role in the antioxidant activity of this plant extract. The findings of this study showed that the chrysanthemum hydroalcoholic extract had very high antioxidant properties due to its phenolic compounds and could be recommended as an antidote to the organophosphate toxins such as paraoxon.