General Information
-
DRAMP ID
- DRAMP01556
-
Peptide Name
- Caerin-1.6 (Frogs, amphibians, animals)
-
Source
- Litoria xanthomera (Orange-thighed frog) (Litoria chloris)
-
Family
- Belongs to the frog skin active peptide family (Caerin subfamily)
-
Gene
- Not found
-
Sequence
- GLFSVLGAVAKHVLPHVVPVIAEKL
-
Sequence Length
- 25
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial,Antiviral
-
Target Organism
-
- [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=2 µM).
-
Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
-
Cytotoxicity
-
- [Ref.26026377]Human endocervical cells End1/E6E7:50% cell death at 10 µM.
-
Binding Target
- Cell membrane
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
-
PDB ID
- None
-
Predicted Structure
- There is no predicted structure for DRAMP01556.
Physicochemical Information
-
Formula
- C124H205N31O29
Absent Amino Acids
- CDMNQRTWY
Common Amino Acids
- V
Mass
- 2594.18
PI
- 8.61
Basic Residues
- 4
Acidic Residues
- 1
Hydrophobic Residues
- 15
Net Charge
- +3
-
Boman Index
- 28.5
Hydrophobicity
- 1.224
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
DRAMP01556
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
- Inhibition of HIV infection by caerin 1 antimicrobial peptides.
-
Pubmed ID
- 26026377
-
Reference
- Peptides. 2015 Sep;71:296-303.
-
Author
- VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.
- ·Literature 2
-
Title
- New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera.
-
Pubmed ID
- 9230483
-
Reference
- J Pept Sci. 1997 May-Jun;3(3):181-185.
-
Author
- Steinborner ST, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ, Ramsay SL.
- ·Literature 3
-
Title
- New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera. Part 2. Sequence determination using mass spectrometry and associated techniques.
-
Pubmed ID
- 9204574
-
Reference
- Rapid Commun Mass Spectrom. 1997;11(9):997-1000.
-
Author
- Steinborner ST, Waugh RJ, Bowie JH, Tyler MJ.
- ·Literature 4
-
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.
-
Pubmed ID
- 9516047
-
Reference
- J Pept Res. 1998 Feb;51(2):121-126.
-
Author
- Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ.