Scorpion venoms contain a variety of peptides toxic to mammals, insects and crustaceans. Among these peptides there is a family of short toxins (30 to 40 residues) [1,2] that currently consist of:

• Inhibitors of calcium-activated and/or voltage-dependent potassium channels such as charybdotoxin (ChTX), iberiotoxin (IbTX), kaliotoxin (KTX), leiurotoxin I (LeTX I), margatoxin (MgTX) or noxiustoxin (NTX)
• Inhibitors of chloride channels such as chlorotoxin.
• Insect toxins such as insectotoxin I1, insectotoxin I5a and neurotoxin P2.

As shown in the following schematic representation, these toxins contain six conserved cysteines involved in disulfide bonds. Our signature pattern contains the last five cysteines.

                             +---------------------+
                             |                     |
                             |     ************************
                      xxxxxxxCxxxxxCxxxCxxxxxxxxxxxCxxxxCxCxxx
                                   |   |                | |
                                   |   +----------------|-+
                                   +--------------------+

'C': conserved cysteine involved in a disulfide bond.
'*': position of the pattern.