Magainin-1 – Potent antimicrobial peptide
Magainin-1 is a 23-amino acids peptide which belongs to the magainin peptide family.
Magainins are antibiotic peptides with antibacterial, antiviral and antifungal activities. These peptides cause perturbation of membrane functions responsible for osmotic balance.
Magainin-1 carries out its antibacterial activity by folding to an amphiphilic helix to interact specifically with lipidic bilayer, resulting in a permeability change.
Magainin-1 has broad-spectrum, non-specific activity against a wide range of micro-organisms including viruses as HSV-1 and HSV-2, gram-positive and gram-negative bacteria, protozoa, yeasts and fungi. Magainin-1 may also be hemolytic and cytotoxic to cancer cells.
Besides its antimicrobial activity, Magainin-1 presents an antifungal activity against some pathogens such as Candida Albicans with a antifungal activity of 4.15 uM. Recently, it has also been shown that magainin-1 can induce apoptosis of some leukemia cells at a concentration of 10 to 50 nM.
|Sequence : GIGKFLHSAGKFGKAFVGEIMKS|
|MW : 2 409.9 Da (C112H177N29O28S)|
|Purity : > 95%|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in propylene 2mL microtubes|
|Other names : magainin 1 peptide, Xenopus, Meganin 1, CHEMBL409372, LS-186859, LS-187515, J-002140, 108433-99-4|
|Peptide Solubility Guideline|
|Bulk peptide quantities available|
|Product catalog||Size||Price € HT||Price $ USD|
1- Jacob L, Zasloff M. Ciba Found Symp. (1994)
Magainins are a family of linear, amphipathic, cationic antimicrobial peptides, 21 to 27 residues in length, found in the skin of Xenopus laevis. They kill microbial targets through disruption of membrane permeability. They exhibit selectivity, on the basis of their affinity for membranes which contain accessible acidic phospholipids, a property characterizing the cytoplasmic membranes of many species of bacteria. Magainins are broad-spectrum antimicrobial agents exhibiting cidal activity against Gram-negative and Gram-positive bacteria, fungi and protozoa. In addition these peptides lyse many types of murine and human cancer cells at concentrations 5-10-fold lower than normal human cells. Because of their selectivity, broad spectrum, low degree of bacterial resistance and ease of chemical synthesis, magainins are being developed as human therapeutic agents. The most advanced candidate is MSI-78, a 22-residue magainin analogue. This peptide is currently in human Phase IIb/III clinical trials in studies intended to evaluate its efficacy as a topical agent for the treatment of impetigo. Preclinical studies have demonstrated that analogues of magainin exhibit activity in vivo against malignant melanoma and ovarian cancer cells in mouse models. Intravenous administration of several magainin analogues has been shown to treat effectively systemic Escherichia coli infections in the mouse.