• Description

  • Application Data


Anti-microbial peptide from the CAMP family. Active against Gram-positive and Gram-negative bacteria, fungi and protozoa and has anti-viral and anti-tumour properties.

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Application Data

Catalogue number crb1000013
Molecular Weight 2466.9
Sequence (one letter code) GIGKFLHSAKKFGKAFVGEIMNS-acid
Sequence (three letter code) H-Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Asn-Ser-OH
Molecular Weight 2466.9
Purity >95%
Storage - 20 ° C

Boohaker et al (2012) The Use of Therapeutic Peptides to Target and to Kill Cancer Cells. Curr. Med. Chem. 19(22) 3794 PMID: 22725698

Pino-Angeles et al (2016) Pore Structure and Synergy in Antimicrobial Peptides of the Magainin Family. PLOS Comput. Biol. 12(1) e1004570 PMID: 26727376

Data Sheet Material Safety Data Sheet (MSDS)

Magainins, also known as PGS (peptide glycine serine) are anti-microbial peptides originally isolated from the skin of the African clawed frog Xenopus laevis, they belong to a large family of amphibian amphipathic α-helical cationic anti-microbial peptides (CAMPs). Magainin II is active against a wide spectrum of pathogens including Gram-positive and Gram-negative bacteria, fungi and protozoa and has anti-viral properties. Magainins also displays anti-tumour activities and are known to facilitate wound closure and to reduce inflammation.

Magainin peptides act by first binding to and then causing eventual collapse of the membrane. Magainins, carry several positive charges, and interact best with membranes with a negative surface charge, such as bacteria or tumour cells. They are non-toxic to healthy eukaryotic cells which are charge-neutral at their outer membrane. The physical mode of action of these peptides reduces the ability of target organisms to develop resistance to them, suggesting good therapeutic potential.

Magainin II

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