Magainin I
GIGKFLHSAGKFGKAFVGEIMK-acid
Description
Application Data
Description
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Anti-microbial peptides from the CAMP family. Active against Gram-positive and Gram-negative bacteria, fungi and protozoa and has anti-viral and anti-tumour properties.
Application Data
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Catalogue number crb1000012 Molecular Weight 2321.3 Sequence (one letter code) GIGKFLHSAGKFGKAFVGEIMK-acid
Sequence (three letter code) H-Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-OH
Purity >95% Storage -20°C References 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
Manufactured in: United Kingdom 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 I is active against a wide spectrum of pathogens including Gram-positive and Gram-negative bacteria, fungi and protozoa and has anti-viral properties against HIV and herpes simplex virus. 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. However 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 is also available in our catalogue.