Magainin 1是在非洲爪蟾皮肤中发现的抗微生物多肽。
Description | Magainin 1 is an antimicrobial peptide discovered in the skin of Xenopus laevis. | ||||||||||||||||
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In Vitro | Magainin 1 kill bacteria by permeabilizing the cell membranes without exhibiting significant toxicity against mammalian cells. The main target of the peptide is considered to be the lipid matrix of the membranes[1]. Magainin 1 and 2 have a similar amino-acid sequence. Magainin 2 has higher antimicrobial activity than magainin 1[2]. 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[3]. Magainin 2 displays antibiotic activity against numerous Gram-negative and Gram-positive bacteria. A similar spectrum of activity is seen on assay of magainin 1[4]. | ||||||||||||||||
Solvent & Solubility | In Vitro: 10 mM in H2O Preparing Stock Solutions
* Please refer to the solubility information to select the appropriate solvent. | ||||||||||||||||
References | |
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