Magainin-2

Magainin-2 is a 23-amino acid antimicrobial peptide originally isolated from the skin of the African clawed frog (Xenopus laevis). It represents one of the most studied antimicrobial peptides with demonstrated activity against parasites, bacteria, fungi, and even some tumor cells.

Magainin-2 adopts an amphipathic alpha-helical structure upon contact with lipid membranes. It creates pores in parasitic and microbial membranes through the 'toroidal pore' model, leading to membrane disruption, ion leakage, and cell death. The peptide preferentially targets negatively charged membranes, sparing host cells.

Rapid membrane binding kinetics. Subject to proteolytic degradation. Various analogs have been developed with improved stability.

Note: These are research protocols from literature. This is not medical advice.

Peptides that may be combined based on complementary mechanisms in research settings.

• 1Effective against Plasmodium falciparum (malaria parasite) at low micromolar concentrations
• 2Demonstrated activity against Leishmania, Giardia, and Trichomonas
• 3Pexiganan, a derivative, reached Phase 3 clinical trials for diabetic foot infections
• 4Minimal resistance development due to membrane-targeting mechanism
• 5Synergistic with conventional antiparasitic agents

Store lyophilized at -20°C. Protect from light.

Scientific References

• 1
  Magainins as paradigm for the mode of action of pore forming polypeptides

  Zasloff M

  Proceedings of the National Academy of Sciences, 1987

• 2
  Antiparasitic activity of magainin analogues

  Guerrero E, et al.

  Antimicrobial Agents and Chemotherapy, 2004