General Information

    • DRAMP ID

    • DRAMP01550

    • Peptide Name

    • Caerin-1.11 (Frogs, amphibians, animals)

    • Source

    • Litoria caerulea (Green tree frog)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • GLLGAMFKVASKVLPHVVPAITEHF

    • Sequence Length

    • 25

    • Protein Existence

    • Homology

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-

    • Target Organism

      • Gram-negative bacteria: Escherichia coli B (MIC=25 µM), Enterobacter cloacae (MIC=50 µM), Klebsiella pneumoniae (MIC=25 µM);
      • Gram-positive bacterium: Staphylococcus haemolyticus (MIC=50 µM).

    • Hemolytic Activity

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

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • 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

    • DRAMP01550 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP01550.

Physicochemical Information

    • Formula

    • C126H201N31O30S

    • Absent Amino Acids

    • CDNQRWY

    • Common Amino Acids

    • V

    • Mass

    • 2662.23

    • PI

    • 8.61

    • Basic Residues

    • 4

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 13

    • Net Charge

    • +3

    • Boman Index

    • 18.26

    • Hydrophobicity

    • 0.896

    • Aliphatic Index

    • 120.8

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 4

DRAMP01550

DRAMP01550 chydropathy plot

Comments Information

    • Function

    • Antibacterial and antiviral peptides that adopt an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity (By similarity).

    • PTM

    • C-terminal amidation.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain.

    • Reference

    • Eur J Biochem. 2003 May;270(9):2068-2081.

    • Author

    • Vanhoye D, Bruston F, Nicolas P, Amiche M.
  • ·Literature 2

    • Title

    • Host-defense peptides of Australian anurans. Part 2. Structure, activity, mechanism of action, and evolutionary significance.

    • Reference

    • Peptides. 2012 Sep;37(1):174-188.

    • Author

    • Bowie JH, Separovic F, Tyler MJ.