The active compounds and AChE inhibitor of the methanol extract of Adonis coerulea maxim against Psoroptes cuniculi.

Adonis coerulea Maxim. presents acaricidal activity in vitro and in vivo, and inhibits AChE and other enzymes activities. However, the active compounds against Psoroptes cuniculi were still unclear. AChE, a common acaricidal and insecticidal target, plays a key role in neural conduction of mites. In this study, using surface plasmon resonance (SPR) technology, AChE was used as a target to capture the compounds from A. coerulea methanol extract (MEAC). After calculating the affinity with molecular docking, the inhibitory effect of compounds against AChE was studied. Results showed that 27 compounds were captured by AChE and identified from MEAC by LC-MS/MS. Among of these compounds, eight compounds presented the high affinity with AChE and high scores in molecular docking assay, especially for silibinin (-12.19 kcal/mol) and vitexin (-11.72 kcal/mol). Further studies showed that although these compounds have the weak cytotoxicity against C6/36 cells, silibinin, quercetin and corilagin could inhibit AChE activity with IC values of 40.11 μg/mL, 46.15 μg/mL and 50.98 μg/mL, respectively. These results indicated that silibinin, quercetin and corilagin may be responsible for AChE inhibition which contributes to the acaricidal properties of A coerulea. This study lays the foundation for developing sensitive and sustainability methods for active compound detection from plants.