Melittin is a 26-amino-acid cationic amphipathic peptide (sequence: GIGAVLKVLTTGLPALISWIKRKRQQ, MW ~2846 g/mol) that constitutes approximately 40-60% of dry honeybee (Apis mellifera) venom. It is the principal active component responsible for the pain, inflammation, and hemolytic activity of bee stings. Melittin has been extensively studied for antimicrobial, anticancer, and anti-inflammatory properties in preclinical settings but is limited therapeutically by its potent cytotoxicity and hemolytic activity.
Category: Antimicrobial / Immune. Evidence rating: D (animal/preclinical only).
Clinical status: Preclinical. Bee venom therapy (apitherapy) is used in traditional medicine. No approved pharmaceutical product based on isolated melittin.
Melittin is an alpha-helical amphipathic peptide that inserts into lipid bilayers, forming toroidal pores that disrupt membrane integrity. At low concentrations it associates with membranes as monomers; at higher concentrations it forms tetrameric pores. This mechanism confers broad-spectrum…
Safety considerations: Highly hemolytic at micromolar concentrations — major limitation for systemic use; Causes intense pain, local inflammation, and edema at injection site; Anaphylaxis risk in bee venom-allergic individuals (potentially life-threatening).
Reviewed by the PeptideAtlas Editorial Team.
| Amino-acid sequence | GIGAVLKVLTTGLPALISWIKRKRQQ |
|---|---|
| Molecular weight | ~2846 g/mol |
| CAS number | 20449-79-0 |
| Production method | bioactive |
| Anti-doping status | not-listed |
| US regulatory status | Not FDA-approved as a drug. Whole bee venom is a licensed biologic for desensitization immunotherapy. Isolated melittin has no approved indication. |
Related peptides: LL-37, Beta-Defensins, Alpha-Defensins.
No. Bee venom (apitherapy) uses whole venom containing many components (melittin, apamin, phospholipase A2, MCD peptide, etc.). Melittin is the single most abundant component (40-60%) but isolated melittin research is distinct from whole bee venom therapy.
Melittin is extremely toxic to all cell types, not just pathogens. Its potent hemolytic activity, cytotoxicity, and pain-inducing properties make systemic administration dangerous. Research focuses on targeted delivery systems (nanoparticles, conjugates) to reduce off-target toxicity.
No. While melittin shows anticancer activity in laboratory and animal studies, it is far too toxic for systemic use in humans. Research is exploring nanoparticle-based delivery to target melittin specifically to tumor cells, but this remains preclinical.
Coverage on this site: Catalog Peptides: Diverse Applications in Biotech and Health.