Bee Secapin is a small antimicrobial peptide (AMP) produced by the venom glands of honeybees (Apis mellifera) and related bee species. Secapin belongs to a group of cationic venom-derived peptides that participate in innate immune defense and antimicrobial activity, functioning alongside other bee antimicrobial peptides such as abaecin, apidaecin, defensin-1, and hymenoptaecin. Structurally, secapin is a short, cysteine-rich peptide stabilized by disulfide bonds, which contributes to its stability and biological activity. Secapin exhibits antimicrobial activity against bacteria and fungi, likely through interactions with microbial membranes that disrupt cell integrity or interfere with cellular processes. In bees, peptides such as secapin help protect the colony and individual insects from microbial infection following injury or venom injection. Because of its broad antimicrobial properties and structural stability, secapin has attracted interest in research on novel antimicrobial compounds, peptide therapeutics, and insect innate immunity, contributing to studies aimed at developing alternative antimicrobial agents and understanding immune defense mechanisms in insects.