General Information

    • DRAMP ID

    • DRAMP01559

    • Peptide Name

    • Caerin-1.8 (Frogs, amphibians, animals)

    • Source

    • Litoria chloris (Blue-thighed frog)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • GLFKVLGSVAKHLLPHVVPVIAEKL

    • Sequence Length

    • 25

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal, Antiviral

    • Target Organism

    • Litoria chloris

    • 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

    • Alpha helix

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP01559 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP01559.

Physicochemical Information

    • Formula

    • C128H214N32O29

    • Absent Amino Acids

    • CDMNQRTWY

    • Common Amino Acids

    • LV

    • Mass

    • 2665.3

    • PI

    • 9.7

    • Basic Residues

    • 5

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 14

    • Net Charge

    • +4

    • Boman Index

    • 22.02

    • Hydrophobicity

    • 0.98

    • Aliphatic Index

    • 159.6

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 3

DRAMP01559

DRAMP01559 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 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 Information

  • ·Literature 1

    • 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.