• DRAMP ID

    • DRAMP01355
    • Peptide Name

    • Ranalexin (Frogs, amphibians, animals)
    • Source

    • Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
    • Family

    • Unknown
    • Gene

    • Unknown
    • Sequence

    • FLGGLIKIVPAMICAVTKKC
    • Sequence Length

    • 20
    • Evidence code

    • Protein level
    • Biological Activity

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

      • Gram-positive bacterium: Staphylococcus aureus (MIC=4 µg/ml);
      • Gram-negative bacteria: Escherichia coli (MIC=32 µg/ml), Pseudomonas aeruginosa (MIC=128 µg/ml).
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Unknown
    • Structure Description

    • Unknown
    • DRAMP01355 helical wheel diagram
    • Formula

    • C97H169N23O22S3
    • Absent Amino Acids

    • DEHNQRSWY
    • Common Amino Acids

    • IK
    • Mass

    • 2444.84
    • PI

    • 9.67
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 10
    • Boman Index

    • 26.85
    • Hydrophobicity

    • 140
    • Aliphatic Index

    • 136.5
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 125
    • Absorbance 280nm

    • 6.58
    • Polar Residues

    • 5

DRAMP01355

DRAMP01355 chydropathy plot
    • Function

    • Potent microbicidal activity, active against S.aureus and E.coli. It acts as well as a membrane-disruptive agent at higher concentrations.
    • Tissue specificity

    • Expressed by the skin dorsal glands.
    • Developmental stage

    • Expression starts at metamorphosis and continues into adulthood.
    • PTM

    • Contains one disulfide bond 14-20.
  • Literature 1
    • Reference

    • J Biol Chem. 1994 Apr 8;269(14):10849-10855.
    • Author

    • Clark DP, Durell S, Maloy WL, Zasloff M.
    • Title

    • Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin.
  • Literature 2
    • Reference

    • Eur J Biochem. 1998 Apr 1;253(1):221-228.
    • Author

    • Vignal E, Chavanieu A, Roch P, Chiche L, Grassy G, Calas B, Aumelas A.
    • Title

    • Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles.