Product Description | Magainin 2 (sequence: GIGKFLHSAKKFGKAFVGEIMNS) is a member of a class of antimicrobial peptides originally discovered in the skin of the African clawed frog (Xenopus laevis) (Zasloff, 1987). These peptides kill bacteria by permeabilizing cell membranes without causing significant toxicity to mammalian cells. Magainin 2 forms toroidal pores in bacterial membranes (~2.8 nm in diameter), leading to leakage of cellular contents and microbial death (Lee et al., 2008). Biologically, magainins are synthesized in the stomach and stored in a novel granular, multinucleated cell in the gastric mucosa. In the skin, they are stored in their active, processed form within the granules of granular gland secretions (Zasloff, 2002). Due to their selective membrane-disruptive action and low mammalian toxicity, Magainin 2 is being explored for applications in treating antibiotic-resistant infections and even certain cancers (Zairi et al., 2018). |
Scientific Background | Magainin 2 is a 23-residue synthetic peptide with the sequence Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Asn-Ser. The sequence contains 4 Lys and 0 Arg residues, contributing cationic character; contains 3 aromatic residues that can contribute to hydrophobic or aromatic interactions. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
