Antimicrobial peptides magainin

Matsuzaki K, Murase O, Fujii N, Miyajima K (1996) An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry-Us 35 11361-11368... 

Another kind of contact-active antimicrobial surface was achieved by tethering antimicrobial peptides to surfaces [62], If such peptides were exclusively membrane-active they could not work like in solution but would be immobilized via a polymeric spacer that could potentially cross the cell wall. The latter was demonstrated by the group of Dathe, who immobilized cationic antimicrobial peptides on PentaGels [63], Also, the well-known antimicrobial peptide magainin I... 

Shi, Y., Cromie, M., Hsu, F., Turk, J., Groisman, E. PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B. Mol Microbiol 53 (2004) 229-241. 

Takeshima, K., Chikushi, A., Lee, K. K., Yonehara, S., and Matsuzaki, K. (2003) Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes. J. Biol. Chem. 278, 1310-1315. 

Duclohier H. Molle C, Spach G. Antimicrobial peptide magainin I from Xenopui skin forms anion-permeable channels in planar lipid bilayers. BiophysJ 1989 56 1017-1021. 

Rana, F.R., and Blazsk, J., 1991, Interactions between the antimicrobial peptide, magainin 2, and Salmonella typhimurium lipopolysaccharides, FEBS 293 11-15. 

Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Nad. Acad. Sci. USA 1987, 84, 5449-5453. 

The amphipathic a-helical class of host defense peptides is the most abundant and most well-characterized class. Upon interaction with the hydrophobic membrane environment, the largely unstructured peptide adopts an amphipathic ct-helical conformation with one helical face containing the majority of the hydrophobic residues, the opposite containing a large proportion of the polar residues. These peptides are often short (<40 amino acids), devoid of cysteine residues, and found to be unstructured or linear in nonhydrophobic environments. Peptides found within this class include the antimicrobial peptide alamethicin, bee venom melittin, the magainins, and the human cathelicidin LL-37. ... 

Haukland, H. H., Ulvatne, H., Sandvik, K., and Vorland, L. H. (2001). The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEES Lett. 508, 389-393. 

Melittin, a 26-amino acid amphipathic a-helical peptide that occurs in bee venom, has recently been found capable of suppressing HIV-1 gene expression. Melittin inhibits HIV-1 infection in both acutely and persistently infected t-lymphoma (KE37/1) and fibroblastoid (LC5) cells at an IC50 of 0.5 to 1.5 iM this effect is apparently mediated by a direct suppressive action on the HIV long terminal repeat (LTR). Antimicrobial peptides such as melittin (honeybees), cecropin (moths), and magainin (frogs) may thus inhibit cell-associated HIV-1 production at the transcription level. 

Line shape analysis of the static 31P NMR spectra and its corresponding CSA values have been successfully used to study the perturbation effect induced by proteins. 31P data for PLs bilayers interacting with antimicrobial peptide (AMP) magainin-2, aurein-3,3, incorporated into structures of supramolecular lipid assemblies such as toroidal pores and thinned bilayers have been reported.90 Various types of PL systems (l-palmitoyl-d3i-2-oleoyl-s -glycero-3-phosphotidylcholine... 

Xenopus laevis is the only frog investigated in this respect. Serotonin and bufotenidin have been isolated fom its skin glands (ref.20).Recently the magainins, antimicrobial peptides with 23 amino acid residues have been isolated (ref. 21) ... 

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