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Open AccessArticle

Molecular Insights into the Potential Insecticidal Interaction of β-Dihydroagarofuran Derivatives with the H Subunit of V-ATPase

by Jielu Wei 1,†, Ding Li 1,†, Xin Xi 1, Lulu Liu 1, Ximei Zhao 1, Wenjun Wu 2 and Jiwen Zhang 1,2,*
1
College of Chemistry & Pharmacy, Northwest A&F University, Yangling 712100, Shaanxi, China
2
Key Laboratory of Botanical Pesticide R&D in Shaanxi Province, Yangling 712100, Shaanxi, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2017, 22(10), 1701; https://doi.org/10.3390/molecules22101701
Received: 11 September 2017 / Revised: 3 October 2017 / Accepted: 6 October 2017 / Published: 11 October 2017
(This article belongs to the Section Bioorganic Chemistry)
Celangulin V (CV), one of dihydroagarofuran sesquiterpene polyesters isolated from Chinese bittersweet (Celastrus angulatus Maxim), is famous natural botanical insecticide. Decades of research suggests that is displays excellent insecticidal activity against some insects, such as Mythimna separata Walker. Recently, it has been validated that the H subunit of V-ATPase is one of the target proteins of the insecticidal dihydroagarofuran sesquiterpene polyesters. As a continuation of the development of new pesticides from these natural products, a series of β-dihydroagarofuran derivatives have been designed and synthesized. The compound JW-3, an insecticidal derivative of CV with a p-fluorobenzyl group, exhibits higher insecticidal activity than CV. In this study, the potential inhibitory effect aused by the interaction of JW-3 with the H subunit of V-ATPase c was verified by confirmatory experiments at the molecular level. Both spectroscopic techniques and isothermal titration calorimetry measurements showed the binding of JW-3 to the subunit H of V-ATPase was specific and spontaneous. In addition, the possible mechanism of action of the compound was discussed. Docking results indicated compound JW-3 could bind well in ‘the interdomain cleft’ of the V-ATPase subunit H by the hydrogen bonding and make conformation of the ligand–protein complex become more stable. All results are the further validations of the hypothesis, that the target protein of insecticidal dihydroagarofuran sesquiterpene polyesters and their β-dihydroagarofuran derivatives is the subunit H of V-ATPase. The results also provide new ideas for developing pesticides acting on V-ATPase of insects. View Full-Text
Keywords: β-dihydroagarofuran; V-ATPase; subunit H of V-ATPase; isothermal titration calorimetry; ITC; fluorescence spectroscopy; molecule docking β-dihydroagarofuran; V-ATPase; subunit H of V-ATPase; isothermal titration calorimetry; ITC; fluorescence spectroscopy; molecule docking
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MDPI and ACS Style

Wei, J.; Li, D.; Xi, X.; Liu, L.; Zhao, X.; Wu, W.; Zhang, J. Molecular Insights into the Potential Insecticidal Interaction of β-Dihydroagarofuran Derivatives with the H Subunit of V-ATPase. Molecules 2017, 22, 1701.

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