Short scorpion toxin chloride channel inhibitors are short-chain neurotoxins (SCNs) (see <PDOC00875>), which block small-conductance chloride channels. They are 30-40-residue long and contain four intramolecular disulfide bridges, which have been assigned as C1-C4, C2-C6, C3-C7 and C5-C8 [1,2,3].

The global fold of the scorpion short toxin chloride channel inhibitor subfamily is an α-helix packed on a two-stranded β-sheet (see <PDB:1CHL>). The structure also contains a short fragment in an extended form. The two antiparalllel β-strands are connected by a type I β-turn. The four disulfide bridges help to maintain a very compact structure by heavily attaching the N-terminal and C-terminal ends to the α-helix [1,2,3].

The scorpion short toxin chloride channel inhibitor subfamily includes:

• Buthus sindicus chlorotoxin-like peptide Bs8 and Bs 14.
• Mesobuthus martensii (Manchurian scorpion) short-chain Cl-channel toxin (BmKCT) and Neurotoxin Bm12-b from (Buthus martensii)
• Buthus eupeus (Lesser Asian scorpion) insectotoxin BeI3, BeI4 and BeI5.
• Parabuthus schlechteri (Scorpion) toxin PBITx1 (sITx10).
• Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) chlorotoxin (CTX).
• Leiurus quinquestriatus hebraeus (Yellow scorpion) probable toxin Lqh-8/6.
• Androctonus mauretanicus mauretanicus (Scorpion) neurotoxin P2.