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Voltage-gated potassium (K V ) channels regulate diverse physiological processes and are an important target for developing novel therapeutic approaches. Sea anemone (Cnidaria, Anthozoa) venoms comprise a highly complex mixture of peptide toxins with diverse and selective pharmacology on K V channels. From the nematocysts of the sea anemone Actinia bermudensis , a peptide that we named AbeTx1 was purified and functionally characterized on 12 different subtypes of K V channels (K V 1.1⁻K V 1.6; K V 2.1; K V 3.1; K V 4.2; K V 4.3; K V 11.1; and, Shaker IR), and three voltage-gated sodium channel isoforms (Na V 1.2, Na V 1.4, and BgNa V ). AbeTx1 was selective for Shaker-related K⁺ channels and is capable of inhibiting K⁺ currents, not only by blocking the K⁺ current of K V 1.2 subtype, but by altering the energetics of activation of K V 1.1 and K V 1.6. Moreover, experiments using six synthetic alanine point-mutated analogs further showed that a ring of basic amino acids acts as a multipoint interaction for the binding of the toxin to the channel. The AbeTx1 primary sequence is composed of 17 amino acids with a high proportion of lysines and arginines, including two disulfide bridges (Cys1⁻Cys4 and Cys2⁻Cys3), and it is devoid of aromatic or aliphatic amino acids. Secondary structure analysis reveals that AbeTx1 has a highly flexible, random-coil-like conformation, but with a tendency of structuring in the beta sheet. Its overall structure is similar to open-ended cyclic peptides found on the scorpion κ-KTx toxins family, cone snail venoms, and antimicrobial peptides.

AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K+ Channels Activation