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Melittin

● Preclinical
Bee Venom Membrane-Disrupting Peptide
Also known as: bee venom peptide, MLT, phospholipase A2 activator
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Quick Summary

Melittin is the primary cytolytic component of bee venom (Apis mellifera), comprising ~50% of dry venom weight. It is a 26-amino acid amphipathic, cationic peptide that forms an alpha-helix in membrane environments and disrupts lipid bilayers via a detergent-like mechanism.

Venom Peptide Preclinical
Melittin is the primary cytolytic component of bee venom (Apis mellifera), comprising ~50% of dry venom weight. It is a 26-amino acid amphipathic, cationic peptide that forms an alpha-helix in membrane environments and disrupts lipid bilayers via a detergent-like mechanism. Melittin has broad antimicrobial, antiviral, anti-inflammatory, and anticancer activities in vitro and in animal models. Its potent hemolytic activity limits systemic use, but nano-encapsulated melittin and melittin-drug conjugates are being developed to exploit its cytotoxic activity against cancer cells.
Storage Stability
Lyophilized
1–2 years (-20°C)
Reconstituted
~30 days (2–8°C)
Room temp
Avoid

Mechanism of Action

Membrane Disruption

Melittin adopts an amphipathic alpha-helical conformation in membrane environments, inserting into lipid bilayers. At low concentrations it forms transient pores (toroidal pore model); at higher concentrations it causes carpet-like membrane solubilization. This mechanism disrupts bacterial, fungal, viral envelopes, and mammalian cell membranes without selectivity, explaining both its broad antimicrobial activity and its hemolytic toxicity.

Intracellular Signaling

Beyond membrane disruption, melittin activates phospholipase A2 (PLA2) indirectly via membrane perturbation, releasing arachidonic acid and initiating prostaglandin/leukotriene synthesis. It inhibits NF-kB and downstream pro-inflammatory cytokines in immune cells. At sub-lytic concentrations, melittin can modulate cell signaling without causing immediate cell death.


Research Summary

Anti-Cancer Activity

Preclinical

Melittin shows cytotoxic activity against numerous cancer cell lines including breast, prostate, lung, and hepatocellular carcinoma. Nano-encapsulated melittin (lipid-coated nanoparticles) selectively targets tumor vasculature. Melittin-drug conjugates (e.g., melittin-paclitaxel) show synergistic anticancer effects in murine tumor models.

Antiviral Activity

Preclinical

Melittin disrupts viral envelopes, showing activity against HIV, HSV, influenza, and HPV in cell culture. Nano-particle formulations sequestering melittin until HIV contact have been developed to maintain antiviral activity while reducing systemic toxicity.

Anti-Inflammatory (Bee Venom Therapy)

Limited Clinical

Bee venom acupuncture (BVA) using dilute bee venom containing melittin shows anti-inflammatory effects in arthritis and Parkinson's disease in pilot clinical trials, involving NF-kB inhibition and regulatory T cell induction.


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Research Protocols

GoalDoseFrequencyRoute
Anticancer cytotoxicity (in vitro)1-20 uMSingle time-point (24-72h)In vitro cell culture
Antimicrobial MIC0.5-32 ug/mLSingle plate readIn vitro broth microdilution
Bee venom therapy (dilute)0.1-1 mg/mL diluted venomAcupuncture point injectionIntradermal/subcutaneous

Systemic melittin is too hemolytic for IV use. Research focuses on encapsulated formulations.


Interactions

co-component
Apamin (bee venom)
Both major bee venom peptides; melittin handles membrane disruption, apamin handles SK channel blockade
synergistic
Phospholipase A2 (bee venom PLA2)
Melittin + PLA2 act synergistically on membrane disruption; together they mediate cytolytic activity of bee venom
synergistic
Paclitaxel
Melittin disrupts cell membranes, enhancing paclitaxel intracellular uptake and cytotoxicity in cancer cells

Safety Profile

Melittin is acutely hemolytic at systemic doses, precluding IV administration. Local injection (bee sting, BVA) causes pain, local inflammation, and edema. Systemic envenomation in sensitive individuals causes anaphylaxis and multi-organ failure. No approved melittin product exists.


References

  • [1]Habermann E. Bee and wasp venoms. Science. 1972;177(4046):314-322.
  • [2]Leuschner C, Bhatt DL. Melittin potently inhibits tumor growth and metastasis. Oncogene. 1996;13(12):2621-2625.
  • [3]Hood JD, et al. Tumor regression by targeted gene delivery to the neovasculature. Science. 2002;296(5577):2404-2407.
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Verified Scientific Data Last audited:
Data Sources & External References
Source: peer-reviewed literature  ·  Domain: ascendpeptide.org

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