Antimicrobial peptides are produced by plants and most organisms throughout the animal kingdom including humans. Antimicrobial peptides protect against a broad range of infectious agents, as bacteria, fungi, and viruses. The amphibian skin is an especially rich source of antimicrobial peptides. See also the product families: Hepcidins LL-37 and Fragments Tuftsin and Analogs (subfamily).
Sapecin originally isolated from the flesh fly Sarcophaga peregrina is a synthetic peptide consisting of 40 amino acids and 3 disulfide bridges. Sapecin has strong antibacterial activity against various Gram-positive bacteria and is also found to stimulate embryonic cell proliferation. Although sapecin shows high homology to charybdotoxin, the high-affinity binding site for charybdotoxin on the potassium channel is not affected by sapecin.