General Information
-
DRAMP ID
- DRAMP01553
-
Peptide Name
- Caerin-1.4 (Frogs, amphibians, animals)
-
Source
- Litoria caerulea (Green tree frog) (also Litoria gilleni) (Centralian tree frog)
-
Family
- Belongs to the frog skin active peptide family (Caerin subfamily)
-
Gene
- Not found
-
Sequence
- GLLSSLSSVAKHVLPHVVPVIAEHL
-
Sequence Length
- 25
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=12 µg/ml), Listeria innocua (MIC=100 µg/ml), Micrococcus luteus (MIC=0.4 µg/ml), Staphylococcus aureus (MIC=100 µg/ml), Staphylococcus epidermis (MIC=25 µg/ml), Streptococcus uberis (MIC=100 µg/ml);
- Gram-negative bacteria: Escherichia coli (MIC=50 µg/ml), Pasteurella multocida (MIC=25 µg/ml). (Ref.2)
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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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
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Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- Please click DRAMP01553_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C120H200N32O32
Absent Amino Acids
- CDFMNQRTWY
Common Amino Acids
- LV
Mass
- 2603.1
PI
- 7.02
Basic Residues
- 4
Acidic Residues
- 1
Hydrophobic Residues
- 13
Net Charge
- +3
-
Boman Index
- 14.34
Hydrophobicity
- 0.972
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
- 5
DRAMP01553
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
- Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.
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Pubmed ID
- 15203252
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Reference
- Peptides. 2004 Jun;25(6):1035-1054.
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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 2
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Title
- Peptides from Australian frogs. The structures of the caerins from Litoria caerula.
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Pubmed ID
- PubMed ID is not available
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Reference
- J. Chem. Res. 1993; 138: 910-936.
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Author
- Stone DJM, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ.