Magainin 1 TFA (Magainin I TFA) is an antimicrobial and amphipathic peptide isolated from the skin of Xenopus laevis. Magainin 1 TFA exhibits antibiotic activity against numerous Gram-negative and Gram-positive bacteria^[1][2][3].

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].

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

2523.87

C₁₁₄H₁₇₈N₂₉F₃O₃₀S

Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser

GIGKFLHSAGKFGKAFVGEIMKS

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [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.

  [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.

  [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.