• DRAMP ID

    • DRAMP02271
    • Peptide Name

    • Magainin-2 (Magainin II; chain of Magainins; Frogs, amphibians, animals)
    • Source

    • Xenopus ruwenzoriensis (Uganda clawed frog)
    • Family

    • Belongs to the gastrin/cholecystokinin family. Magainin subfamily.
    • Gene

    • N/A
    • Sequence

    • GIGKFLHSAKKFGKAFVGEIMNS
    • Sequence Length

    • 23
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal
    • Target Organism

      • Gram-negative bacteria: Escherichia coli D31 (MIC=5 µg/ml), Klebsiella pneumoniae (MIC=10 µg/ml), Escherichia coli (MIC=50 µg/ml), Pseudomonas putida (MIC=10 µg/ml), Citrobacter freundii (MIC=30 µg/ml), Enterobacter cloacae (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Serratia marcescens (MIC=100 µg/ml), Proteus mirabilis (MIC>100 µg/ml);
      • Gram-positive bacteria: Staphylococcus epidermidis (MIC=10 µg/ml), Staphylococcus aureus (MIC=50 µg/ml), Streptococcus fecalis (MIC>100 µg/ml).
      • Protozoa: Paramecium caudatum (MIC=10 µg/ml).
      • Yeast: Candida albicans (MIC=80 µg/ml).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Alpha helix
    • Structure Description

    • The secondary structure is shown to be helical in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.
    • Helical Wheel Diagram

    • DRAMP02271 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP02271.
    • Formula

    • C114H180N30O29S
    • Absent Amino Acids

    • CDPQRTWY
    • Common Amino Acids

    • GK
    • Mass

    • 2466.93
    • PI

    • 10
    • Basic Residues

    • 5
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +4
    • Boman Index

    • -9.64
    • Hydrophobicity

    • 0.083
    • Aliphatic Index

    • 72.17
    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 7

DRAMP02271

DRAMP02271 chydropathy plot
    • Function

    • Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.
    • Tissue specificity

    • Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. It is stored as active, processed peptides in large granules within the granular gland secretions of the skin.
  • ·Literature 1
    • Title

    • Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.
    • Reference

    • Proc Natl Acad Sci U S A. 1987 Aug;84(15):5449-5453.
    • Author

    • Zasloff M.
  • ·Literature 2
    • Title

    • Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.
    • Reference

    • J Biomol NMR. 1997 Feb;9(2):127-135.
    • Author

    • Gesell J, Zasloff M, Opella SJ.
  • ·Literature 3
    • Title

    • All Atom Simulations of the Initial Binding of Magainin and Pleurocidin to Membranes Comprising a Mixture of Anionic and Zwitterionic
    • Reference

    • To be Published.
    • Author

    • Vermeer LS, Kozlowska J, Lorenz CD, Mason JA.