kv4.2

BmP02, a compound isolated from Chinese scorpion (Buthus martensi Karsch) venom, acts as a selective Kv1.3 channel blocker and a highly-selective Kv4.2 modulator. It delays Kv4.2 inactivation in HEK293T cells, exhibiting an EC50 of approximately 850 nM, and inhibits the transient outward potassium currents (Ito) in ventricular muscle cells [1] [2].

Heteropodatoxin-2, a 30-amino acid peptide, inhibits the Kv4.2 current in Xenopus laevis oocytes through a voltage-dependent mechanism, exhibiting reduced blocking at more positive potentials [1].

Phrixotoxin 2 selectively blocks the KV 4.2 and KV 4.3 channels, demonstrating high specificity in its interaction with these voltage-gated ion channels [1].

Jingzhaotoxin-V, a 29-residue polypeptide from Chilobrachys jingzhao spider venom, selectively inhibits tetrodotoxin-resistant and tetrodotoxin-sensitive sodium currents in rat dorsal root ganglion neurons, with IC50 values of 27.6 nM and 30.2 nM, respectively. Furthermore, it suppresses Kv4.2 potassium currents in Xenopus laevis oocytes, with an IC50 of 604.2 nM [1].

Jingzhaotoxin-X (JZTX-X) selectively inhibits Kv4.2 and Kv4.3 potassium channels, resulting in prolonged mechanical hyperalgesia [1].

Heteropodatoxin-1 (HpTx1), a spider peptide toxin, acts as an inhibitor of the Kv4.2 current, while concurrently inhibiting Nav1.7 and activating Nav1.9 channels. However, it has no effect on Nav1.8 channels [1].