• DRAMP ID

    • DRAMP01355
    • Peptide Name

    • Ranalexin (Frogs, amphibians, animals)
    • Source

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

    • Not found
    • Gene

    • Not found
    • Sequence

    • FLGGLIKIVPAMICAVTKKC
    • Sequence Length

    • 20
    • Protein Existence

    • Protein level
    • Biological Activity

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

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

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Cyclization (Cys14 and Cys20)
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys14 and Cys20.
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01355 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01355.
    • Formula

    • C97H169N23O22S3
    • Absent Amino Acids

    • DEHNQRSWY
    • Common Amino Acids

    • IK
    • Mass

    • 2105.73
    • PI

    • 9.39
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 10
    • Net Charge

    • +3
    • Boman Index

    • 26.85
    • Hydrophobicity

    • 1.4
    • 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
    • Title

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

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

    • Clark DP, Durell S, Maloy WL, Zasloff M.
  • ·Literature 2
    • Title

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