| Name
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Dermaseptin
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| Sequence (Single letter abbreviations)
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ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ
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| Sequence（Three letter abbreviations）
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{ALA}{LEU}{TRP}{LYS}{THR}{MET}{LEU}{LYS} {LYS}{LEU}{GLY}{THR}{MET}{ALA}{LEU}{HIS} {ALA}{GLY}{LYS}{ALA}{ALA}{LEU}{GLY}{ALA} {ALA}{ALA}{ASP}{THR}{ILE}{SER}{GLN}{GLY} {THR}{GLN}
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| Basic description
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Dermaseptins are antimicrobial peptides, strings of amino acids, or proteins, of various sizes and shapes. Dermaseptins were isolated from frog skin. Dermaseptin is a crucial part of the frog's immune system, inhibiting the growth of bacteria, protozoa and fungi. Dermaseptins are cationic (positively charged) and 27-34 residues in length. Dermaseptins adopt a largely K-helical conformation when binding to membranes. Like other antimicrobial peptides, dermaseptin is membrane-perturbing; however, unlike other antimicrobial peptides, dermaseptin rests on the surface of the bacterial membrane and does not insert.
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| The molecular weight
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3455.100
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| Chemical formula
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C152H257N43O44S2
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| The purity
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> 95%
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| Storage conditions
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Store at -20°C. Keep tightly closed. Store in a cool dry place.
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| Annotation
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ly potent antimicrobial activity against pathogenic fungi.
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| Documents
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| Figures
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| Reference
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Rydlo T, et al. Antibacterial properties of dermaseptin S4 derivatives under extreme incubation conditions. Antimicrob. Agents Chemother. Feb 2006; 50(2): 490-497.
Shalev DE, et al. Consequences of N-acylation on structure and membrane binding properties of dermaseptin derivative K4-S4-(1-13). J. Biol. Chem. Apr 2006; 281(14): 9432-9438.
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Dermaseptin
