Molecular Diversity and Isoform Evolution in Venom: Insights from Proteomic Analysis.

Over millions of years of evolution, natural selection has driven the specialization of predatory and defensive mechanisms in various animal species through the development of poisons and venoms. These venoms contain highly specific and selective molecules for several different targets according to the habitat and behavior of each species. In this work, we performed a comprehensive proteomic analysis of venom, identifying 45 proteins, including 8 toxins targeting K channels, 22 targeting Na channels, and 15 other venom components. Our study reveals seven novel isoforms of ion channel-targeting peptides characterized by amino acid substitutions which may influence their bioactivity and pharmacological properties. These findings contribute to our understanding of venom molecular diversity and evolution, providing new insights into peptide structure-function relationships. Considering the biomedical relevance of ion channel-modulating toxins, our work expands the repertoire of potential candidates for future drug development, particularly in the context of neuropharmacology and ion channel disorders.