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A textbook cationic amphipathic AMP from frog skin that helped launch the AMP field.
Also known as: magainin 2 · magainin II
Part of the Foundational & therapeutic peptides cluster
Overview
Magainins are cationic antimicrobial peptides from the skin of the African clawed frog, with magainin 2 (GIGKFLHSAKKFGKAFVGEIMNS) the best-studied member. They fold into amphipathic alpha-helices in membranes and disrupt microbial cell membranes, making them a classic model in antimicrobial-peptide research.
Source & context
Biological / chemical source: Skin of the African clawed frog (Xenopus laevis)
Primary research or clinical context: Antimicrobial-peptide research (not an approved drug)
Discovery and structure
Magainins were discovered in Xenopus laevis skin in the late 1980s. They are largely unstructured in water but adopt an amphipathic alpha-helix on contact with membranes, separating cationic and hydrophobic faces — the hallmark architecture of many host-defense peptides.
Why researchers study it
Magainin 2 is a reference AMP for studying membrane permeabilization, pore formation and broad-spectrum activity against bacteria, fungi and protozoa. It underpins ongoing design of synthetic analogs and is not an approved therapeutic.
Sequence
One-letter sequence commonly cited for Magainin (educational; isoforms and modifications may differ):
GIGKFLHSAKKFGKAFVGEIMNS
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
- Magainin (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
- PubChem molecular record · 2026-10-01
- Molecular formula
- C114H180N30O29S
- Average reference mass
- ≈ 2,466.9
- PubChem CID: 16130189
- CAS RN: 108433-95-0
Chemistry values: PubChem · fetched 2026-10-01.
Magainin — 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: Magainin (source record; form not independently established)Average reference mass: 2,466.9 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 Magainin
What is Magainin?+
Magainins are cationic antimicrobial peptides from the skin of the African clawed frog, with magainin 2 (GIGKFLHSAKKFGKAFVGEIMNS) the best-studied member. They fold into amphipathic alpha-helices in membranes and disrupt microbial cell membranes, making them a classic model in antimicrobial-peptide research.
What Canadian product status is recorded for Magainin?+
Canadian product status for Magainin 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 Magainin?+
Magainin is commonly described as approximately 23 amino acids (Antimicrobial peptide).
Related peptides
References & further reading
- 1.Kabelka et al. (2020). Magainin 2 and PGLa in Bacterial Membrane Mimics II: Membrane Fusion and Sponge Phase Formation. Biophys J
- 2.Goto et al. (2019). Development of Amphipathic Antimicrobial Peptide Foldamers Based on Magainin 2 Sequence. ChemMedChem
- 3.Kabelka et al. (2022). Magainin 2 and PGLa in bacterial membrane mimics III: Membrane fusion and disruption. Biophys J
- 4.Montero Vega et al. (2022). Interaction between Antimicrobial Peptide Magainin 2 and Nonlipid Components in the Bacterial Outer Envelope. J Phys Chem B
- 5.Ludtke et al. (1996). Membrane pores induced by magainin. Biochemistry
- 6.Billah et al. (2023). Antimicrobial peptide magainin 2-induced rupture of single giant unilamellar vesicles comprising E. coli polar lipids. Biochim Biophys Acta Biomembr
- 7.Syryamina et al. (2024). Self-assembly of spin-labeled antimicrobial peptides magainin 2 and PGLa in lipid bilayers. Biophys Chem
- 8.Lehmann et al. (2006). Antitumor activity of the antimicrobial peptide magainin II against bladder cancer cell lines. Eur Urol
- 9.PubChem — compound summary for Magainin 2 (CID 16130189)
- 10.Wikipedia — Magainin