Eucalyptus globulus leaf-isolated isorhapontin serves as a natural insecticide via acetylcholinesterase inhibition
Copyright © 2024. Published by Elsevier Inc..
Acetylcholinesterase (AChE) inhibitors cause insect death by preventing the hydrolysis of the neurotransmitter acetylcholine, which overstimulates the nervous system. In this study, isorhapontin, isolated from E. globulus leaves, was evaluated as a natural insecticide with AChE inhibition at 12.5 μM. Using kinetic analyses, we found that isorhapontin acted as a competitive inhibitor that binds to the active site of AChE. The inhibition constant (Ki) was 6.1 μM. Furthermore, isorhapontin and resveratrol, which have basic skeletons, were predicted to bind to the active site of AChE via molecular docking. A comparison of the hydrogen bonding between the two stilbenes revealed characteristic differences in their interactions with amino acids. In isorhapontin, Trp83, Gly149, Tyr162, Tyr324, and Tyr370 interacted with the sugar moiety. These results suggest that with further development, isorhapontin can be used as an insecticide alternative.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:200 |
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| Enthalten in: |
Pesticide biochemistry and physiology - 200(2024) vom: 06. März, Seite 105834 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Park, Jae Yeon [VerfasserIn] |
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| Links: |
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| Themen: |
Acetylcholinesterase |
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| Anmerkungen: |
Date Completed 08.04.2024 Date Revised 08.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.pestbp.2024.105834 |
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| 520 | |a Acetylcholinesterase (AChE) inhibitors cause insect death by preventing the hydrolysis of the neurotransmitter acetylcholine, which overstimulates the nervous system. In this study, isorhapontin, isolated from E. globulus leaves, was evaluated as a natural insecticide with AChE inhibition at 12.5 μM. Using kinetic analyses, we found that isorhapontin acted as a competitive inhibitor that binds to the active site of AChE. The inhibition constant (Ki) was 6.1 μM. Furthermore, isorhapontin and resveratrol, which have basic skeletons, were predicted to bind to the active site of AChE via molecular docking. A comparison of the hydrogen bonding between the two stilbenes revealed characteristic differences in their interactions with amino acids. In isorhapontin, Trp83, Gly149, Tyr162, Tyr324, and Tyr370 interacted with the sugar moiety. These results suggest that with further development, isorhapontin can be used as an insecticide alternative | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Acetylcholinesterase | |
| 650 | 4 | |a Eucalyptus globulus leaves | |
| 650 | 4 | |a Isorhapontin | |
| 650 | 4 | |a Molecular docking | |
| 650 | 4 | |a Natural insecticide | |
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| 650 | 7 | |a Insecticides |2 NLM | |
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| 650 | 7 | |a Cholinesterase Inhibitors |2 NLM | |
| 650 | 7 | |a Stilbenes |2 NLM | |
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| 700 | 1 | |a Lee, Gihwan |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Kwang Dong |e verfasserin |4 aut | |
| 700 | 1 | |a Lee, Sang Won |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Jeong Yoon |e verfasserin |4 aut | |
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