Scorpine-like peptides are intriguing and unique compounds of scorpion venom. They possess two well-defined regions that confers them bi-functionality. The N-terminal region is similar to scorpion antimicrobial peptides lacking disulfide bridges, whereas the C-terminal region contains six cysteines forming three disulfide bridges that tightly bind the peptide. Scorpine-like peptides have shown activity against bacteria (i.e. B. subtilis, K. pneumoniae, P. aeruginosa), fungi and also as potassium channel blockers. Additionally, they have been successful in controlling malaria and some types of viruses.