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IMMUNEPEPTIDE PROFILE

Magainin

Also known as Magainin-2, Magainin 2a, MSI-78 (analog), Pexiganan (analog)

Magainin is a family of broad-spectrum antimicrobial peptides isolated from the skin of the African clawed frog Xenopus laevis, first characterized by Michael Zasloff in 1987. Magainin-2 is the primary studied isoform — a 23-amino acid cationic peptide with activity against gram-positive and gram-negative bacteria, fungi, and protozoa. It was the first frog-derived AMP to enter clinical development.

Last updated April 10, 2026

TL;DR

Quick summary

Magainin is a broad-spectrum antimicrobial peptide from frog skin (Xenopus laevis) that established foundational principles of membrane-disrupting AMP drug design. Its analog pexiganan reached Phase III trials for diabetic foot ulcers but failed to achieve superiority over standard antibiotics.

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Overview

Magainin is a family of broad-spectrum antimicrobial peptides isolated from the skin of the African clawed frog Xenopus laevis, first characterized by Michael Zasloff in 1987. Magainin-2 is the primary studied isoform — a 23-amino acid cationic peptide with activity against gram-positive and gram-negative bacteria, fungi, and protozoa. It was the first frog-derived AMP to enter clinical development.

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Mechanism of action

In aqueous solution, magainin-2 is largely unstructured. Upon contact with negatively charged bacterial membranes, it folds into an amphipathic alpha-helix and inserts into the bilayer via a 'carpet model' or toroidal pore mechanism. At sufficient concentrations, magainin causes membrane thinning, transient pore formation, and eventually membrane disintegration and leakage of cytoplasmic contents. Selectivity for prokaryotic over eukaryotic membranes arises from the abundance of anionic phospholipids in bacterial outer leaflets versus zwitterionic phosphatidylcholine-dominated mammalian membranes.

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Dosing protocols

PurposeRouteDosageFrequency
antimicrobial researchtopical10100 mcg/mLresearch use only

Dosing information is for educational purposes only. Consult a qualified healthcare professional before using any peptide.

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Research summary

Magainin research established foundational principles of AMP membrane disruption, influencing drug design of hundreds of synthetic analogs. A magainin analog (pexiganan/MSI-78) reached Phase III trials for diabetic foot ulcer infections but failed to achieve superiority versus standard antibiotic comparators (1999), partly due to regulatory endpoint requirements. Research continues on magainin structural analogs with improved potency and reduced toxicity. Magainin-2 remains a gold-standard positive control in AMP research.[1][2][3][4]

📄This section cites 4 peer-reviewed sources. View all references →
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Evidence grading

Each claimed benefit is graded by the strength of available evidence. Grades reflect study quality, not effect size.

strong
First frog-derived AMP characterizedFoundational Zasloff 1987 PNAS work establishing magainin-2 structure/function
strong
Disrupts membranes via carpet/toroidal pore mechanismExtensive biophysics and molecular dynamics studies of membrane interaction
strong
Broad-spectrum antibacterial and antifungal activityHundreds of in vitro MIC studies across gram-positive, gram-negative, fungi
strong
Pexiganan failed Phase III for diabetic foot ulcersCompleted 1999 Phase III trial failed superiority versus standard antibiotics
moderate
Selective for prokaryotic over eukaryotic membranesConsistent anionic phospholipid selectivity studies; narrow therapeutic window

Strong = multiple RCTs · Moderate = limited trials or observational · Preliminary = animal or in vitro only · Insufficient = anecdotal or no published data

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Side effects

Hemolytic at high concentrations
Cytotoxicity to mammalian cells above therapeutic window

Side effects vary by individual. This is not an exhaustive list. Report unusual symptoms to a healthcare professional.

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Common stacks

Peptides commonly paired with Magainin for synergistic effects.

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Sourcing & access

Research compound

Magainin is classified as a research compound. Regulatory status varies by jurisdiction. Always verify current legal status and source from vendors providing third-party certificates of analysis (COA).

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Frequently asked questions

Magainin is a family of antimicrobial peptides first isolated from the skin of the African clawed frog Xenopus laevis in 1987. Magainin-2, a 23-amino acid cationic peptide, is the primary studied isoform with activity against gram-positive and gram-negative bacteria, fungi, and protozoa.

Magainin-2 folds into an amphipathic alpha-helix upon contact with bacterial membranes and disrupts them via carpet model or toroidal pore mechanisms. It selectively targets prokaryotic membranes due to their abundance of anionic phospholipids, sparing mammalian cells at therapeutic concentrations.

Magainin can be hemolytic at high concentrations and cytotoxic to mammalian cells above the therapeutic window. Its selectivity for bacterial over mammalian membranes provides a therapeutic index, but this was insufficient for the clinical analog pexiganan to gain FDA approval.

Pexiganan (MSI-78), a synthetic magainin analog, reached Phase III trials for diabetic foot ulcer infections in 1999 but failed to demonstrate superiority versus standard antibiotic comparators, partly due to regulatory endpoint requirements. Magainin-2 remains a gold-standard control in AMP research.

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Research references

  1. Magainins: antimicrobial peptides from Xenopus skin with broad spectrum activityZasloff M, et al.Proc Natl Acad Sci USA, 1987PubMed
  2. Mechanism of action of magainin peptides: membrane permeabilizationMatsuzaki K, Murase O, et al.Biochemistry, 1995PubMed
  3. Magainin and related peptides as anticancer agents and membrane disruptorsCruciani RA, Barker JL, et al.Proc Natl Acad Sci USA, 1991PubMed
  4. Frog-skin antimicrobial peptides: diversity, structure, and therapeutic prospectsConlon JM, et al.Biochim Biophys Acta, 2021PubMed
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