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108433-99-4

108433-99-4 structure
108433-99-4 structure
  • Name: Magainin 1
  • Chemical Name: magainin i
  • CAS Number: 108433-99-4
  • Molecular Formula: C112H177N29O28S
  • Molecular Weight: 2409.85000
  • Catalog: Peptides
  • Create Date: 2018-06-19 16:49:46
  • Modify Date: 2024-01-02 19:37:42
  • Magainin 1 is an antimicrobial peptide discovered in the skin of Xenopus laevis.

Name magainin i
Synonyms GLY-ILE-GLY-LYS-PHE-LEU-HIS-SER-ALA-GLY-LYS-PHE-GLY-LYS-ALA-PHE-VAL-GLY-GLU-ILE-MET-LYS-SER
Gly-L-Ile-Gly-L-Lys-L-Phe-L-Leu-L-His-L-Ser-L-Ala-Gly-L-Lys-L-Phe-Gly-L-Lys-L-Ala-L-Phe-L-Val-Gly-L-Glu-L-Ile-L-Met-L-Lys-L-Ser-OH
MAGAININ 1 (FROG,XENOPUS LAEVIS)
H-GLY-ILE-GLY-LYS-PHE-LEU-HIS-SER-ALA-GLY-LYS-PHE-GLY-LYS-ALA-PHE-VAL-GLY-GLU-ILE-MET-LYS-SER-OH
GIGKFLHSAGKFGKAFVGEIMKS
Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser-OH
MAGAININ 1
Description Magainin 1 is an antimicrobial peptide discovered in the skin of Xenopus laevis.
Related Catalog
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].
References

[1]. Matsuzaki K, et al. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim Biophys Acta. 1998 Nov 10;1376(3):391-400.

[2]. Watanabe H, et al. Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method. Anal Sci. 2016;32(1):57-60.

[3]. 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.

[4]. 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.

Molecular Formula C112H177N29O28S
Molecular Weight 2409.85000
Exact Mass 2408.30000
PSA 939.34000
LogP 4.96870
Storage condition -20°C
Personal Protective Equipment Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter
Hazard Codes T+
RIDADR NONH for all modes of transport
WGK Germany 3