General Information

    • DRAMP ID

    • DRAMP01565

    • Peptide Name

    • Caerin-2.4 (Frogs, amphibians, animals)

    • Source

    • Litoria caerulea (Green tree frog)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • GLVSSIGKALGGLLADVVKTKEQPA

    • Sequence Length

    • 25

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

    • No MICs found in DRAMP database

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP01565 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP01565.

Physicochemical Information

    • Formula

    • C109H191N29O34

    • Absent Amino Acids

    • CFHMNRWY

    • Common Amino Acids

    • GL

    • Mass

    • 2451.89

    • PI

    • 8.5

    • Basic Residues

    • 3

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 11

    • Net Charge

    • +1

    • Boman Index

    • -1.18

    • Hydrophobicity

    • 0.4

    • 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

DRAMP01565

DRAMP01565 chydropathy plot

Comments Information

    • 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 Information

  • ·Literature 1

    • 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.