Androctonus Research Articles

Scorpion venom: pharmacological analysis and its applications

Scorpions belong to class: Arachnida, order: Scorpionida represented now by approximately 1500 species. These are one of the most ancient group of the animals on the earth conserving their morphology almost unaltered and are the most successful inhabitants of the earth. Scorpions when stimulated secrete venom which is a cocktail of variable concentration of neurotoxins, cardiotoxins, nephrotoxins, hemolytic toxins, phosphodiesterases, phospholipases, hyaluronidase, glucosaminoglycans, histamine, seratonin, tryptophan and cytokine releasers. According to an estimate, frequency of deaths caused by scorpion sting is higher in comparison to that of caused by snake-bite. Almost all of these lethal scorpions except Hemiscorpious species belong to scorpion family Buthidae comprising 500 species. Scorpion venoms show variable reactions in envenomated patients. However, closer the phylogenic relationship among the scorpions, more similar the immunological properties. Furthermore, various constituents of venom may act directly or indirectly and individually or synergistically to exert their effects. Scorpion stings cause a wide range of conditions from severe local skin reactions to neurologic, respiratory and cardiovascular collapse. Lethal members of Buthidae family include Buthus , Parabuthus , Mesobuthus , Tityus , Leiurus , Androctonus and Centruroides . Besides their lethal properties, scorpion venoms have some unique properties beneficial to mankind. These contain anti-insect, antimicrobial and anticancer properties and thus, can play a key role in the insect pest management programmes, treatment of microbial infection and in the treatment of various cancer types.

Amino Acid Sequence of an Excitatory Insect-selective Toxin (BmK IT) From Venom of the Scorpion Buthus martensi Karsch

The insect-selective neurotoxin(BmK IT) of scorpion Buthus martensi Karsch was first reduced and S-alkylated, and then digested by TPCK-trypsin and Staphylococcus aureus V-8 Protease. The enzymatic peptides were purified on TLC-plastic sheet and submitted to determine their amino acid compositions and sequences. The sequence of the 70 amino acid residues of BmK IT was established with reference to the primary structure of AaH IT, another excitatory insect-selective toxin from the venom of North African scorpion Androctonus australis Hector. About 75% of the homologous sequence was found in the molecules of BmK IT and AaH IT. It is obvious that the results contribute toward better understanding of the molecular structure characteristics, structure/activity relationship of scorpion insect-selective toxins, and they can serve as the molecular basis for utilizing the toxins as a tool to clarify molecular mechanism involved in channel gating, and to infer the possibility of developing them as new selective bioinsecticides.