General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.