• DRAMP ID

    • DRAMP01557
    • Peptide Name

    • Caerin-1.7 (Frogs, amphibians, animals)
    • Source

    • Litoria xanthomera (Orange-thighed frog) (Litoria chloris)
    • Family

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

    • Not found
    • Sequence

    • GLFKVLGSVAKHLLPHVAPVIAEKL
    • Sequence Length

    • 25
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial,Antiviral
    • Target Organism

      • [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2.5 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

    • Cell membrane
    • 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

    • DRAMP01557 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01557.
    • Formula

    • C126H210N32O29
    • Absent Amino Acids

    • CDMNQRTWY
    • Common Amino Acids

    • L
    • Mass

    • 2637.25
    • PI

    • 9.7
    • Basic Residues

    • 5
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 14
    • Net Charge

    • +4
    • Boman Index

    • 19.79
    • Hydrophobicity

    • 0.884
    • Aliphatic Index

    • 152
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 3

DRAMP01557

DRAMP01557 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 dorsal 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

    • New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera.
    • Reference

    • J Pept Sci. 1997 May-Jun;3(3):181-185.
    • Author

    • Steinborner ST, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ, Ramsay SL.
  • ·Literature 3
    • Title

    • New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera. Part 2. Sequence determination using mass spectrometry and associated techniques.
    • Reference

    • Rapid Commun Mass Spectrom. 1997;11(9):997-1000.
    • Author

    • Steinborner ST, Waugh RJ, Bowie JH, Tyler MJ.
  • ·Literature 4
    • Title

    • New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria.
    • Reference

    • J Pept Res. 1998 Feb;51(2):121-126.
    • Author

    • Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ.