Magainin 2
Magainin 2 structure
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Common Name | Magainin 2 | ||
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| CAS Number | 108433-95-0 | Molecular Weight | 2466.90000 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C114H180N30O29S | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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Trypanosoma cruzi: synergistic cytotoxicity of multiple amphipathic anti-microbial peptides to T. cruzi and potential bacterial hosts.
Exp. Parasitol. 125(4) , 342-7, (2010) The parasite Trypanasoma cruzi is responsible for Chagas disease and its triatomine vector, Rhodnius prolixus, has a symbiotic relationship with the soil bacterium, Rhodococcus rhodnii. R. rhodnii that was previously genetically engineered to produce the anti... |
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Design and characterization of novel hybrid antimicrobial peptides based on cecropin A, LL-37 and magainin II.
Peptides 33(2) , 197-205, (2012) Antimicrobial peptides (AMPs) are a naturally occurring component of the innate immune response of many organisms and can have activity against both Gram-negative and Gram-positive bacterial species. In order to optimize and improve the direct antimicrobial e... |
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Magainins as paradigm for the mode of action of pore forming polypeptides.
Biochim. Biophys. Acta 1376 , 391-400, (1998) Magainins are a class of antimicrobial peptides discovered in the skin of Xenopus laevis. The peptides kill bacteria by permeabilizing the cell membranes without exhibiting significant toxicity against mammalian cells, and are a promising candidate for a new ... |
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Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure.
Biochemistry 38 , 10377, (1999) Magainins are positively charged amphiphatic peptides which permeabilize cell membranes and display antimicrobial activity. They are usually thought to bind specifically to anionic lipids, and binding studies have been performed almost exclusively with negati... |
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A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides.
FEBS Lett. 449 , 105, (1999) The hemolytic and fungicidal activity of a number of cationic antimicrobial peptides was investigated. Histatins and magainins were inactive against human erythrocytes and Candida albicans cells in phosphate buffered saline, but displayed strong activity agai... |
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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. 84 , 5449, (1987) A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis. It consists of two closely related peptides that are each 23 amino acids and differ by two substitutions. These peptides... |
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Action of antimicrobial peptides: two-state model.
Biochemistry 39 , 8347, (2000) The argument and experimental evidence are presented for a two-state model that explains the action of both helical and beta-sheet antimicrobial peptides after they bind to the plasma membranes of cells. Each peptide has two distinct physical states of bindin... |
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The cationic peptide magainin II is antimicrobial for Burkholderia cepacia-complex strains.
J. Med. Microbiol. 58(Pt 7) , 923-9, (2009) This study was undertaken to determine the antibacterial activity of eight cationic antimicrobial peptides towards strains of genomovars I-V of the Burkholderia cepacia complex (Bcc) in time-kill assays. All but one of the peptides failed to show activity aga... |
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Antimicrobial peptide P18 inhibits inflammatory responses by LPS- but not by IFN-gamma-stimulated macrophages.
Biotechnol. Lett. 30(7) , 1183-7, (2008) Antimicrobial peptide P18 markedly inhibited the expression of inducible nitric oxide synthase (iNOS), tumor necrosis factor-alpha (TNF-alpha) and interleukin-1 beta (IL-1beta) in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells, whereas magainin... |
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Use of a real-time polymerase chain reaction thermocycler to study bacterial cell permeabilization by antimicrobial peptides.
Anal. Biochem. 381(2) , 279-81, (2008) Antimicrobial peptides are good leads to develop new antibiotics, but knowledge of their mode of action is a prerequisite. Destruction of the microbial membranes through a detergent-like mechanism is one of these modes of action. This is usually studied by us... |