MedChemExpress - Model Magainin 1 -108433-99-4
Magainin 1 (Magainin I) is an antimicrobial and amphipathic peptide isolated from the skin of Xenopus laevis. Magainin 1 exhibits antibiotic activity against numerous Gram-negative and Gram-positive bacteria[1][2][3].MCE products for research use only. We do not sell to patients.
Magainin 1
MCE China：Magainin 1
Brand：MedChemExpress (MCE)
Cat. No.HY-P0269
CAS：108433-99-4
Synonyms：Magainin I
Purity：99.90%
Storage：Sealed storage, away from moisture Powder -80°C 2 years -20°C 1 year *In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)
Shipping：Room temperature in continental US; may vary elsewhere.
Description：Magainin 1 (Magainin I) is an antimicrobial and amphipathic peptide isolated from the skin of Xenopus laevis. Magainin 1 exhibits antibiotic activity against numerous Gram-negative and Gram-positive bacteria.
In Vitro：Magainin 1 interacts with acidic lipids through electrostatic interactions followed by hydrophobic interactions to form an amphiphilic helix, inducing the leakage. Magainin 1 induces the leakage of calcein specifically out of negatively-charged vesicles. The peptide binds to bovine brain phosphatidylserine sonicated vesicles according to the Langmuir isotherm with a binding constant of 3.8×105 M-1 and a binding-site number of 0.10 per lipid molecule[2].
Sequence：Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser
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References：
[1]. Duclohier H, et al. Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys J. 1989 Nov;56(5):1017-21. [Content Brief]
[2]. Matsuzaki K, et al. Magainin 1-induced leakage of entrapped calcein out of negatively-charged lipid vesicles. Biochim Biophys Acta. 1989 May 19;981(1):130-4. [Content Brief]
[3]. Zasloff M, et al. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5449-53. [Content Brief]
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