Much of our knowledge on K+-channels was elucidated using specific peptide ligands isolated from a number of venomous organisms. Recently, this field received a strong support and increased interest due to the solution of the three-dimensional structure of a couple of K+-channels. At the same time, several new subfamilies of specific toxins for K+-channels were isolated from scorpion venoms, enhancing the availability and diversity of such useful molecular tools. It opened new lines of research for the better understanding of K+-channel biophysics and pharmacology. In this review, we listed 120 amino acid sequences of peptides isolated from scorpion venoms. They were demonstrated or assumed to be specific for K+-channels. These sequences were aligned and used to generate a rooted phylogenetic tree. The evolutionary tree indicates that several clusters of divergent peptides show preference for specific subtypes of channels. The three-dimensional structures of representative examples of these peptides were drawn and analysed concerning the molecular fitness of their interactions with the channel targets. Four different interacting modes were identified to exist between scorpion toxins and the various subtypes of K+-channels.