• DRAMP ID

    • DRAMP01555
    • Peptide Name

    • Caerin-1.5 (Frogs, amphibians, animals)
    • Source

    • Litoria caerulea (Green tree frog)
    • Family

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

    • Not found
    • Sequence

    • GLLSVLGSVVKHVIPHVVPVIAEHL
    • Sequence Length

    • 25
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=3 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=12 µg/ml), Staphylococcus aureus (MIC=25 µg/ml), Staphylococcus epidermis (MIC=25 µg/ml), Streptococcus uberis (MIC=50 µg/ml);
      • Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml).
      • [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=3 µM).
    • Hemolytic Activity

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

      • [Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 12.5 µM.
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01555 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01555.
    • Formula

    • C123H206N32O30
    • Absent Amino Acids

    • CDFMNQRTWY
    • Common Amino Acids

    • V
    • Mass

    • 2613.19
    • PI

    • 7.02
    • Basic Residues

    • 4
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 14
    • Net Charge

    • +3
    • Boman Index

    • 28.35
    • Hydrophobicity

    • 1.312
    • Aliphatic Index

    • 178.8
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP01555

DRAMP01555 chydropathy plot
    • Function

    • Antibacterial 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.
    • Domain

    • Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity).
    • PTM

    • C-terminal amidation.
  • ·Literature 1
    • Title

    • Inhibition of HIV infection by caerin 1 antimicrobial peptides.
    • Reference

    • Peptides. 2015 Sep;71:296-303.
    • Author

    • VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.
  • ·Literature 2
    • 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 3
    • 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.