ABSTRACT
A peptide toxin was isolated from the venom of Palamneus gravimanus, the Indian black scorpion, to block human Kv1.1 channels expressed in Xenopus laevis oocytes. A 4.5 kD peptide (toxin), as confirmed by SDS-PAGE, was purified to homogeneity by ion exchange chromatography using CM-Sephadex C-25 followed by Sephadex G-50 gel filtration. Palamneus gravimanus toxin (PGT) selectively blocks the human cloned voltage-gated potassium channel hKv1.1 in a two-electrode voltage-clamp (TEVC) technique. The results obtained indicate that the toxin blocks the hKv1.1 channel at a nanomolar concentration range (Ki value of 10 nM) of the peptide to the external side of the cell. The blockage seems to be voltage-dependent. Comparative structure of PGT (a 4.5 kD peptide) with BTK-2 suggests a close relationship; therefore this toxin can be employed to investigate the hKv1.1 channel structure.