• DRAMP ID

    • DRAMP01563
    • Peptide Name

    • Caerin-2.2 (Frogs, amphibians, animals)
    • Source

    • Litoria gilleni (Centralian tree frog) (also Litoria caerulea) (Green tree frog)
    • Family

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

    • Not found
    • Sequence

    • GLVSSIGRALGGLLADVVKSKEQPA
    • Sequence Length

    • 25
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-positive bacterium: Micrococcus luteus (MIC=50 µg/ml);
      • Gram-negative bacterium: Pasteurella multocida (MIC=25 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

    • DRAMP01563 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01563.
    • Formula

    • C108H189N31O34
    • Absent Amino Acids

    • CFHMNTWY
    • Common Amino Acids

    • GL
    • Mass

    • 2465.88
    • PI

    • 8.59
    • Basic Residues

    • 3
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 11
    • Net Charge

    • +1
    • Boman Index

    • -11.38
    • Hydrophobicity

    • 0.372
    • Aliphatic Index

    • 124.8
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 7

DRAMP01563

DRAMP01563 chydropathy plot
    • Function

    • Antimicrobial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.
    • Tissue specificity

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

    • Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.
    • Reference

    • Peptides. 2004 Jun;25(6):1035-1054.
    • Author

    • Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.
  • ·Literature 2
    • Title

    • Peptides from Australian frogs. The structures of the caerins from Litoria caerula.
    • Reference

    • J. Chem. Res. 1993; 138: 910-936.
    • Author

    • Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ.