• DRAMP ID

    • DRAMP01362
    • Peptide Name

    • Frenatin-3 (Frogs, amphibians, animals)
    • Source

    • Litoria infrafrenata (Giant tree frog) (White-lipped tree frog)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • GLMSVLGHAVGNVLGGLFKS
    • Sequence Length

    • 20
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacterium: Escherichia coli (MIC=50 µg/ml);
      • Gram-positive bacteria: Leuconostoc mesenteroides (MIC=25 µg/ml), Bacillus cereus (MIC=12.5 µg/ml), Micrococcus luteus (MIC=1.5 µg/ml), Pastewella haemolytica (MIC=0.8 µg/ml), Streptococcus uberis (MIC=50 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

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01362 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C88H146N24O24S
    • Absent Amino Acids

    • CDEIPQRTWY
    • Common Amino Acids

    • G
    • Mass

    • 1956.33
    • PI

    • 8.76
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +2
    • Boman Index

    • 19.99
    • Hydrophobicity

    • 1.005
    • Aliphatic Index

    • 126.5
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 8

DRAMP01362

DRAMP01362 chydropathy plot
    • Function

    • Wide spectrum antimicrobial peptide. Considered to interact with the outer lipid layer of the bacterial cell, penetrate the bacterial membrane, form ion channels, and ultimately kill the cell.
    • Tissue specificity

    • Expressed by the skin parotoid and/or rostral glands.
  • ·Literature 1
    • Title

    • The structures of the frenatin peptides from the skin secretion of the giant tree frog Litoria infrafrenata.
    • Reference

    • J Pept Sci. 1996 Mar-Apr;2(2):117-124.
    • Author

    • Raftery MJ, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ.