Melittin
The main weapon in bee venom — a powerful membrane-disrupting peptide being repurposed as an antimicrobial and anticancer research tool.
A 26-amino-acid amphipathic alpha-helical peptide comprising ~50% of honeybee venom dry weight that forms pores in lipid bilayers, producing potent cytolytic, antimicrobial, and anticancer activity.
Mechanism of action
Forms toroidal pores (~2.5 nm) in lipid bilayers. Unlike selective AMPs, melittin is cytolytic to both bacterial and mammalian cells. Activates phospholipase A2 and causes mast cell degranulation (bee sting pain). Cancer research exploits its lytic activity with tumor-targeting delivery systems.
Primary uses
- Research: membrane biophysics
- Anticancer research (nanoparticle conjugates)
- Broad-spectrum antimicrobial research
- Template for selective AMP design
Typical dosing
Not used clinically due to non-selective cytotoxicity.
Regulatory status
Not approved. In preclinical development for targeted anticancer therapy (melittin-loaded nanoparticles).
References
- [pubmed] Habermann E. "Bee and wasp venoms." Science. 1972;177(4046):314-322.
- [pubmed] Duffy C, et al. "Honeybee venom and melittin suppress growth factor receptor activation in HER2-enriched and triple-negative breast cancer." NPJ Precis Oncol. 2020;4:24.
Related peptides
This entry is for educational purposes only and does not constitute medical advice. Dosing information reflects published regulatory or research data and is not a recommendation. Many compounds described here are not approved for human use in the United States. Consult a licensed medical professional before considering any peptide therapy.