Different toxins acting on the Kv1.3 channel are isolated from animal venom. MeuKTX toxin from Mesobuthus eupeusEupeus scorpion and the shtx-k toxin from Stichodactyla haddoniHaddoni sea anemone have been identified as two effective Kv1.3 channel blockers. In this work, we have characterized the genomic organization of both toxins. MeuKTX gene contains one intron and two exons, similar to most scorpion toxins. There are a few reports of the genomic structure of sea anemone toxins acting on Kv channels. The sequence encoding the mature peptide of shtx-k washas been located in an exon separated by an intron from the coding exon of the propeptide and signal region. In order to make a peptide with more affinity for the Kv1.3 channel and greater stability, the shtx-k/ MeuKTX chimeric peptide was designed and constructed using the SOE-PCR method. Molecular docking studies indicated more inhibitory effect of shtx-k/MeuKTX on Kv1.3 channel compared to shtx-k and MeuKTX toxins. Key amino acids binding channels from both toxins, alsoare also involved in interactioninteractions of chimeric peptidepeptides with the channel. MeuKTX, shtx-k and shtx-k/MeuKTX waswere cloned and the expression of the soluble proteins in E. coli were determined. Our results showed that the fusion peptide, shtx-k/MeuKTX could be an effective agent to target the Kv1.3 channel.