Magainin 1

Modify Date: 2025-08-27 08:37:53

Magainin 1 structure	Common Name	Magainin 1
	CAS Number	108433-99-4	Molecular Weight	2409.85000
	Density	N/A	Boiling Point	N/A
	Molecular Formula	C₁₁₂H₁₇₇N₂₉O₂₈S	Melting Point	N/A
	MSDS	Chinese USA	Flash Point	N/A

Use of Magainin 1

Magainin 1 is an antimicrobial peptide discovered in the skin of Xenopus laevis.

Name	magainin i
Synonym	More Synonyms

Description	Magainin 1 is an antimicrobial peptide discovered in the skin of Xenopus laevis.
Related Catalog	Signaling Pathways >> Anti-infection >> Bacterial Signaling Pathways >> Anti-infection >> Fungal Peptides Research Areas >> Infection Natural Products >> Others
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

Targeting methicillin-resistant Staphylococcus aureus with short salt-resistant synthetic peptides.

Antimicrob. Agents Chemother. 58(7) , 4113-22, (2014)

The seriousness of microbial resistance combined with the lack of new antimicrobials has increased interest in the development of antimicrobial peptides (AMPs) as novel therapeutics. In this study, we...

In vitro efficacy of a synthetic all-d antimicrobial peptide against clinically isolated drug-resistant strains.

Int. J. Antimicrob. Agents 35(2) , 208-9, (2010)

NMR structural studies of membrane proteins.

Curr. Opin. Struct. Biol. 8(5) , 640-8, (1998)

The three-dimensional structures of membrane proteins are essential for understanding their functions, interactions and architectures. Their requirement for lipids has hampered structure determination...

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

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Dayang Chem (Hangzhou) Co., Ltd.
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Product Name: MAGAININ I
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Magainin 1

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