Page data last changed: . Chemistry registry snapshot: . Registry refreshes and identity assessments are separate from scientific content review.
The main pain-producing peptide of bee venom and a classic model for membrane-lytic activity.
Part of the Foundational & therapeutic peptides cluster
Overview
Melittin is the principal component of honeybee venom, a 26-residue amphipathic peptide that inserts into and permeabilizes lipid membranes. It is a foundational model for studying pore formation and membrane lysis and is investigated for antimicrobial and anticancer research. It is a research compound, not an approved drug.
Source & context
Biological / chemical source: Honeybee venom (Apis mellifera)
Primary research or clinical context: Membrane and antimicrobial research (not an approved drug)
Structure and lytic action
Melittin (GIGAVLKVLTTGLPALISWIKRKRQQ) has a hydrophobic N-terminus and a basic, hydrophilic C-terminus, with no disulfide bonds. This amphipathic layout lets it partition into membranes and form pores, making it a standard reference for membrane-disruption studies.
Research directions and caution
Laboratory studies examine melittin's antimicrobial and anticancer activity, but its strong lytic action toward many cell types complicates any therapeutic use. Educational coverage here focuses on its chemistry and mechanism, not human application.
Sequence
One-letter sequence commonly cited for Melittin (educational; isoforms and modifications may differ):
GIGAVLKVLTTGLPALISWIKRKRQQ
Residues plotted ~100° apart around an α-helix — clustering of one color reveals an amphipathic face.
Structure & chemistry
Molecular identity & reference confidence
Source-supported reference
Reference values are taken from the cited molecular record or curated profile. A database match is not independent laboratory verification; modifications, counter-ions, and formulations can change the measured mass.
- Molecular form
- Melittin (source record; form not independently established)
- Species
- Not established by this molecular identity audit
- Termini (N / C)
- Not specified / Not specified
Average reference mass
Reference policy updated: 2026-10-05
- IUPHAR/BPS source snapshot · 2026-10-01
- PubChem molecular record · 2026-10-01
- Molecular formula
- C131H229N39O31
- Average reference mass
- ≈ 2,846.5
- PubChem CID: 16133648
- IUPHAR ligand: 14002
- ChEMBL: CHEMBL412927
- CAS RN: 20449-79-0
- UNII: 24VT8NVE75
Chemistry values: PubChem, IUPHAR/BPS Guide to Pharmacology · fetched 2026-10-01.
Melittin — reconstitution calculator
Enter how much peptide is in the vial and how much diluent (e.g. bacteriostatic water) is added. The tool returns the resulting solution concentration — and, for any amount you type, the volume it corresponds to. This is educational arithmetic, not a dosing recommendation.
Reference form: Melittin (source record; form not independently established)Average reference mass: 2,846.5 Da
Enter an amount to see the volume it corresponds to.
Educational concentration mathematics only. This tool does not recommend a dose, amount, or protocol, and nothing here is medical advice. Many peptides are not authorized by Health Canada for human use — see our reconstitution and bacteriostatic-water guides for context.
FAQ about Melittin
What is Melittin?+
Melittin is the principal component of honeybee venom, a 26-residue amphipathic peptide that inserts into and permeabilizes lipid membranes. It is a foundational model for studying pore formation and membrane lysis and is investigated for antimicrobial and anticancer research. It is a research compound, not an approved drug.
What Canadian product status is recorded for Melittin?+
Canadian product status for Melittin has not been verified in this profile. No verified record here does not mean no authorization exists. Status depends on the product, formulation and use; consult Health Canada's product records.
What is the typical length of Melittin?+
Melittin is commonly described as approximately 26 amino acids (Membrane-active peptide).
Related peptides
References & further reading
- 1.Duffy et al. (2020). Honeybee venom and melittin suppress growth factor receptor activation in HER2-enriched and triple-negative breast cancer. NPJ Precis Oncol
- 2.Memariani et al. (2019). Melittin: from honeybees to superbugs. Appl Microbiol Biotechnol
- 3.Memariani et al. (2020). Anti-fungal properties and mechanisms of melittin. Appl Microbiol Biotechnol
- 4.Wu et al. (2025). Melittin suppresses ovarian cancer growth by regulating SREBP1-mediated lipid metabolism. Phytomedicine
- 5.Chen et al. (2016). Melittin, the Major Pain-Producing Substance of Bee Venom. Neurosci Bull
- 6.Raghuraman et al. (2007). Melittin: a membrane-active peptide with diverse functions. Biosci Rep
- 7.Guha et al. (2021). Applications and evolution of melittin, the quintessential membrane active peptide. Biochem Pharmacol
- 8.Wang et al. (2025). Melittin inhibits osteosarcoma growth in vitro and in vivo by inactivating the Wnt/β-catenin signaling pathway. J Cancer
- 9.PubChem — compound summary for Melittin (CID 16133648)
- 10.Wikipedia — Melittin