• DRAMP ID

    • DRAMP01549
    • Peptide Name

    • Caerin-1.1 (Frogs, amphibians, animals)
    • Source

    • Litoria splendida (Magnificent tree frog) (Litoria gilleni) (Litoria caerulea)
    • Family

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

    • Unknow
    • Sequence

    • GLLSVLGSVAKHVLPHVVPVIAEHL
    • Sequence Length

    • 25
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Antiviral
    • Target Organism

      • Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=1.5 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12.5 µg/ml), Staphylococcus aureus (MIC=3-12 µg/ml), Staphylococcus epidermis (MIC=12.5 µg/ml), Streptococcus uberis (MIC=12.5 µg/ml);
      • Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml). (Ref.3)
    • Hemolytic activity

    • Unknown
    • Binding Traget

    • Cell membrane
    • Structure

    • Alpha helix
    • Structure Description

    • The peptide adopts two well-defined helices from Leu2 to Lys11 and from Val17 to His24 separated by a region of less-defined helicity and greater flexibility.
    • PDB ID

    • Unknow
    • DRAMP01549 helical wheel diagram
    • Formula

    • C121H202N32O30
    • Absent Amino Acids

    • CDFMNQRTWY
    • Common Amino Acids

    • V
    • Mass

    • 3013.42
    • PI

    • 7.81
    • Basic Residues

    • 4
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 14
    • Boman Index

    • 26.12
    • Hydrophobicity

    • 118.8
    • Aliphatic Index

    • 171.2
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP01549

DRAMP01549 chydropathy plot
    • Function

    • Antibacterial and antiviral peptides that adopt an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.
    • Tissue specificity

    • Secreted by the skin parotoid and/or rostral glands.
    • Domain

    • Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility.
    • Miscellaneous

    • Caerin 1.1 completely inhibits HIV infection of T cells within minutes of exposure to virus at concentrations that were not toxic to target cells (J Virol. 2005 Sep;79(18)
    • PTM

    • C-terminal amidation.
  • Literature 1
    • Reference

    • Eur J Biochem. 1997 Jul 15;247(2):545-557.
    • Author

    • Wong H, Bowie JH, Carver JA.
    • Title

    • The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida.
  • Literature 2
    • Reference

    • J. Chem. Soc. Perkin Trans. I. 1992;1:3173-3178.
    • Author

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

    • Peptides from Australian frogs. Structures of the caerins and caeridin 1 from Litoria splendida.
  • Literature 3
    • 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.
    • Title

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