A Novel Sea Anemone Peptide Ed-79 Blocks Shaker Kv Channels and Exhibits Insecticidal Activity
- 1Hainan Key Laboratory for Research and Development of Tropical Herbs, Engineering Research Center of Tropical Medicine Innovation and Transformation of Ministry of Education, College of Pharmacy, Hainan Medical University, Haikou 571199, China
- 2School of Agricultural and Rural Affairs, Hainan Open University, Haikou 570028, China
- 3Department of Pharmacy, Cangnan Hospital of Wenzhou Medical University, Wenzhou 325800, China
Abstract
The escalating resistance of agricultural pests to conventional chemical insecticides has created an urgent need for eco-friendly biological alternatives with novel modes of action. Sea anemone venoms are rich in structurally stable and target-specific ion channel-modulating peptides, representing a promising source of new insecticidal molecules. Through bioinformatics screening of the transcriptome database of the sea anemone Exaiptasia diaphana, we identified a novel 37-residue peptide, Ed-79, which contains three disulfide bonds. The peptide was chemically synthesized via solid-phase peptide synthesis (SPPS) and successfully folded into its correct disulfide-bonded form using a three-step oxidative folding strategy, as confirmed by LC-MS and RP-HPLC. Circular dichroism (CD) spectroscopy revealed marked secondary-structural changes upon oxidative folding, notably an increased β-sheet content. In insecticidal bioassays, Ed-79 exhibited dose-dependent lethality against Spodoptera frugiperda and Tenebrio molitor, with LD50 values of 289.5 and 367.2 pmol/g, respectively. Molecular docking further predicted that Ed-79 binds stably to the outer vestibule of the Shaker Kv channel pore via eight hydrogen bonds, with Pro475 and Asn482 potentially serving as key interacting residues. Collectively, this is the first systematic report on the synthesis, oxidative folding, insecticidal activity, and predicted Shaker Kv channel-binding mode of Ed-79, providing a solid foundation for developing new insecticidal lead compounds and broadening the utility of anemone venoms as insecticide resources.
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BibTeX
@article{yue2026novel,
title = {{A Novel Sea Anemone Peptide Ed-79 Blocks Shaker Kv Channels and Exhibits Insecticidal Activity}},
author = {Mengxin Yue and Yanling Liao and Tianru Hu and Qin Chen and Xuefeidan Liu and Bingmiao Gao and Qiqi Guo},
journal = {Molecules},
year = {2026},
month = oct,
doi = {10.3390/molecules31213822},
url = {https://www.mdpi.com/1420-3049/31/21/3822},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - A Novel Sea Anemone Peptide Ed-79 Blocks Shaker Kv Channels and Exhibits Insecticidal Activity
AU - Mengxin Yue
AU - Yanling Liao
AU - Tianru Hu
AU - Qin Chen
AU - Xuefeidan Liu
AU - Bingmiao Gao
AU - Qiqi Guo
PY - 2026
DA - 2026/10/23
JO - Molecules
DO - 10.3390/molecules31213822
UR - https://www.mdpi.com/1420-3049/31/21/3822
AB - The escalating resistance of agricultural pests to conventional chemical insecticides has created an urgent need for eco-friendly biological alternatives with novel modes of action. Sea anemone venoms are rich in structurally stable and target-specific ion channel-modulating peptides, representing a promising source of new insecticidal molecules. Through bioinformatics screening of the transcriptome database of the sea anemone Exaiptasia diaphana, we identified a novel 37-residue peptide, Ed-79, which contains three disulfide bonds. The peptide was chemically synthesized via solid-phase peptide synthesis (SPPS) and successfully folded into its correct disulfide-bonded form using a three-step oxidative folding strategy, as confirmed by LC-MS and RP-HPLC. Circular dichroism (CD) spectroscopy revealed marked secondary-structural changes upon oxidative folding, notably an increased β-sheet content. In insecticidal bioassays, Ed-79 exhibited dose-dependent lethality against Spodoptera frugiperda and Tenebrio molitor, with LD50 values of 289.5 and 367.2 pmol/g, respectively. Molecular docking further predicted that Ed-79 binds stably to the outer vestibule of the Shaker Kv channel pore via eight hydrogen bonds, with Pro475 and Asn482 potentially serving as key interacting residues. Collectively, this is the first systematic report on the synthesis, oxidative folding, insecticidal activity, and predicted Shaker Kv channel-binding mode of Ed-79, providing a solid foundation for developing new insecticidal lead compounds and broadening the utility of anemone venoms as insecticide resources.
SN - 1420-3049
ER -