Nematicidal activity of tirotundin and parthenolide isolated from Tithonia diversifolia and Chrysanthemum parthenium

Abstract

Acetylcholinesterase (AChE) is an enzyme that catalyzes acetylcholine into choline and acetic acid. Conventional pesticides, including organophosphates and carbamates target and inhibit the activity of AChE. To obtain more pesticide precursors that meet the safety requirements, more than 200 compounds were screened. Tirotundin and parthenolide identified as potential neurotoxins to nematodes were isolated from Tithonia diversifolia and Chrysanthemum parthenium, respectively. Their IC₅₀ values were 6.89 ± 0.30 and 5.51 ± 0.23 μg/mL, respectively against the AChE isolated from Caenorhabditis elegans. AChE was inhibited in a dose-dependent manner using the two compounds. And the Lineweaver-Burk and Dixon plots indicated that tirotundin and parthenolide were reversible inhibitors against AChE, both inhibiting AChE in a mixed-type competitive manner and demonstrating these compounds may possess dual binding site AChE inhibitors. LC₅₀ values of tirotundin and parthenolide against C. elegans were 9.16 ± 0.21 and 7.23 ± 0.48 μg/mL, respectively. These results provide a certain theoretical basis for the development and utilization of novel pesticides.

Keywords:

• Parthenolide
• tirotundin
• acetylcholinesterase
• enzyme kinetics
• toxic effects

Data availability statement

Data available within the article or its supplementary materials.

Additional information

Funding

This research was supported financially by grants from the Reserve Talents for Yunnan Young and Middle-aged Academic and Technical Leaders (202105AC160037), Natural Science Foundation of Yunnan Province (202001AT070053 and 202001AT070055), grants of State Key Laboratory of Phytochemistry and Plant Resources in West China (P2018-ZZ05 and P2019-ZZ06).