• DRAMP ID

    • DRAMP02009
    • Peptide Name

    • Brevinin-1 (Frogs, amphibians, animals)
    • Source

    • Rana brevipoda porsa (Japanese frog)
    • Family

    • Belongs to the frog skin active peptide family (Brevinin subfamily)
    • Gene

    • Not found
    • Sequence

    • FLPVLAGIAAKVVPALFCKITKKC
    • Sequence Length

    • 24
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.1449472]Gram-positive bacterium: Staphylococcus aureus (MIC=8 µg/ml);
      • Gram-negative bacterium: Escherichia coli (MIC=34 µg/ml).
    • Hemolytic Activity

      • [Ref.1449472] high hemolytic activity
    • 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 (Cys18 and Cys24)
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys18 and Cys24.
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP02009 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02009.
    • Formula

    • C121H204N28O26S2
    • Absent Amino Acids

    • DEHMNQRSWY
    • Common Amino Acids

    • AK
    • Mass

    • 2531.24
    • PI

    • 9.7
    • Basic Residues

    • 4
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 14
    • Net Charge

    • +4
    • Boman Index

    • 28.65
    • Hydrophobicity

    • 1.288
    • Aliphatic Index

    • 134.17
    • Half Life

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

    • 125
    • Absorbance 280nm

    • 5.43
    • Polar Residues

    • 4

DRAMP02009

DRAMP02009 chydropathy plot
    • Function

    • Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and a very high hemolytic activity.
  • ·Literature 1
    • Title

    • Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa.
    • Reference

    • Biochem Biophys Res Commun. 1992 Nov 30;189(1):184-190.
    • Author

    • Morikawa N, Hagiwara K, Nakajima T.