Biochemical Characterization and Cytotoxicity of Heterometrus xanthopus (Scorpion) Venom

Abstract

Scorpion venoms are the sea of bioactive peptide catalogue that offer promising molecules that may give rise to the revelation and development of novel drugs. Heterometrus xanthopus is the most venomous animal, produces potent venoms that aggravate harsh symptoms in envenomated prey. The present investigation, the peptide profile of venom was studied by electrophoretic methods, size-exclusion (FPLC) and reverse phase chromatography. Cytotoxicity of venom was assessed on human corneal endothelial cell line (HCEC) and breast cancer cell line (MCF-7) by using 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl tetrazolium bromide (MTT) assay. Reverse phase High performance liquid chromatography (RP-HPLC) of crude venom helped us to see the complexity present in venom. A number of peaks isolated from venom on different retention time with absorbance. The size exclusion chromatography- Fast protein liquid chromatography (SEC-FPLC) and SDS-page analysis elucidated that the H. xanthopus venom contain high molecular weight peptides ranging from 139.3 to 44.77 kDa as well as low molecular weight peptides ranging from 11.37 to 8.64 kDa. Biomodal mass distribution peaking between molecular weights of 1 to 20 kDa (57%) and 61 kDa to 80 (17%). This statement confirmed the presence of low molecular weight peptides in abundance. H. xanthopus venom had cytotoxic effect on MCF-7 cells and HCEC cell, among all fractions, fraction 7 that contain low molecular weight peptides have great cytotoxic effect, which may explain by presence of low molecular weight toxins in scorpion’s venoms. The present work represented the first peptidomic characterization of H. xanthopus venom. Contemplate the molecular weight-function relationship of already identified venom peptides, future bioactivity studies may lead to the discovery of potassium and chloride ion channel inhibitors as well as antimicrobial peptides from H. xanthopus venom.