General Information
-
DRAMP ID
- DRAMP01554
-
Peptide Name
- Caerin-1.4.1 (Chain of Caerin-1.4)
-
Source
- Litoria caerulea (Green tree frog)
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Family
- Belongs to the frog skin active peptide (FSAP) family (Caerin subfamily)
-
Gene
- Not found
-
Sequence
- GLLSSLSSVA
-
Sequence Length
- 10
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial
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Target Organism
- No MICs found in DRAMP database
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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
-
- Not included yet
-
Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
-
N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
-
Nonterminal Modifications and Unusual Amino Acids
- Not included yet
-
Stereochemistry
- Not included yet
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- There is no predicted structure for DRAMP01554.
Physicochemical Information
-
Formula
- C40H72N10O15
Absent Amino Acids
- CDEFHIKMNPQRTWY
Common Amino Acids
- S
Mass
- 933.07
PI
- 5.52
Basic Residues
- 0
Acidic Residues
- 0
Hydrophobic Residues
- 5
Net Charge
- 0
-
Boman Index
- 7.95
Hydrophobicity
- 1.38
Aliphatic Index
- 156
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 5
DRAMP01554
Comments Information
Function
- Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.
Literature Information
- ·Literature 1
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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.