Isolation and Purification of a Sodium Channel-Targeting Peptide from Buthotus Schach Scorpion Venom Peptide: Characterization of Hsch1 Toxin

Scorpion venom contains polypeptides that modulate ion channel functions. This study focused on isolating and purifying a novel long-chain peptide targeting the sodium channel from the venom of the Iranian scorpion, Buthotus schach. The venom was initially subjected to gel filtration on a Sephadex G-50 column, followed by further purification using reverse-phase high-performance liquid chromatography (RP-HPLC). The purity of the fractions was confirmed via SDS-PAGE electrophoresis, and molecular mass determination was conducted. The chromatographic process yielded a purified toxic peptide, designated as Hsch1, with an LD50 value of 2.17 ± 0.03 μg. Mass spectrometry (MALDI TOF/TOF) revealed the molecular weight of Hsch1 to be 7.2 kDa. The findings suggest that the isolated low-molecular-weight peptide possesses neurotoxic properties, warranting its introduction as a toxic peptide derived from B. Schach scorpion venom.