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APETx1, a New Toxin from the Sea Anemone Anthopleura elegantissima, Blocks Voltage-Gated Human Ether-a-go-go–Related Gene Potassium Channels

Institut de Pharmacologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique (CNRS)-Unité Mixte Recherche 6097, Valbonne, France (S.D., M.L.); Institut de Biologie Structurale et Microbiologie, CNRS Unité Propre de Recherche 9027, Marseille, France (E.L.); and the Klinikum der Christian-Albrechts-Universität, Abteilung Toxikologie, Kiel, Germany (T.B., L.B.)

A new peptide, APETx1, which specifically inhibits human ether-a-go-go–related gene (HERG) channels, was purified from venom of the sea anemone Anthopleura elegantissima. APETx1 is a 42-amino acid peptide cross-linked by three disulfide bridges and shares 54% homology with BDS-I, another sea anemone K⁺ channel inhibitor. Although they differ in their specific targets, circular dichroism spectra and molecular modeling indicate that APETx1 and BDS-I have a common molecular scaffold and belong to the same structural family of K⁺ channel blocking peptides. APETx1 inhibits HERG currents in a heterologous system with an IC₅₀ value of 34 nM by modifying the voltage dependence of the channel gating. Central injections in mice failed to induce any neurotoxic symptoms. APETx1, which has no sequence homologies with scorpion toxins acting on HERG, defines a new structural group of HERG gating modifiers isolated from a sea anemone.

Address correspondence to: Prof. Michel Lazdunski, Institut de Pharmacologie moléculaire et Cellulaire, CNRS- UMR6097, 660 Route des Lucioles, Sophia-Antipolis, 06560 Valbonne, France. E-mail: ipmc{at}ipmc.cnrs.fr

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