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.