General Information
-
DRAMP ID
- DRAMP02818
-
Peptide Name
- Dicynthaurin
-
Source
- Halocynthia aurantium (Sea peach)
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Family
- Not found
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Gene
- Not found
-
Sequence
- ILQKAVLDCLKAAGSSLSKAAITAIYNKIT
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Sequence Length
- 30
-
UniProt Entry
- P0C007
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- [Ref.11479030]Gram-positive bacteria: Micrococcus luteus, Staphylococcus aureus(50 units at 100ug/ml), Listeria monocytogenes(50 units at 40ug/ml);
- Gram-negative bacteria: Escherichia coli(50 units at 10ug/ml), Pseudomonas aeruginosa(25 units at 20ug/ml).
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Hemolytic Activity
-
- [Ref.11479030]10% hemolytic activity at 50 μg/ml, 20% hemolytic activity at 100 μg/ml against human red blood cells
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Cytotoxicity
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
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Nonterminal Modifications and Unusual Amino Acids
- Not included yet
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Stereochemistry
- Not included yet
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Structure
- Alpha helix (CD)
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Structure Description
- CD spectra of the cynthaurin monomer (Fig. 5A) and homodimer (Fig. 5B) in PBS showes properties characteristic of helical peptides. In structure-promoting environments, such as TFE:phosphate buffer or SDS micelles, the helical conformations are enhanced and accounted for the dominant structural component of both the monomeric and the homodimeric peptides.
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Helical Wheel Diagram
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PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP02818.
Physicochemical Information
-
Formula
- C139H242N36O41S
Absent Amino Acids
- EFHMPRW
Common Amino Acids
- A
Mass
- 3105.73
PI
- 9.52
Basic Residues
- 4
Acidic Residues
- 1
Hydrophobic Residues
- 15
Net Charge
- +3
-
Boman Index
- -2.1
Hydrophobicity
- 0.637
Aliphatic Index
- 133.67
Half Life
-
- Mammalian:20 hour
- Yeast:30 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 1490
Absorbance 280nm
- 51.38
Polar Residues
- 9
DRAMP02818
Comments Information
Function
- Shows antibacterial activity against both Gram-positive and Gram-negative bacteria. Its antimicrobial activity is optimal at NaCl concentrations below 100 mM, suggesting that the antimicrobial actions of this peptide may take place intracellularly rather than extracellularly. Has no activity against the fungus C.albicans. Has hemolytic activity.
PTM
- Contians one disulfide bond and C-terminal amidation.
Literature Information
- ·Literature 1
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Title
- Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium.
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Pubmed ID
- 11479030
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Reference
- Biochim Biophys Acta. 2001 Aug 15;1527(3):141-148.
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Author
- Lee IH, Lee YS, Kim CH, Kim CR, Hong T, Menzel L, Boo LM, Pohl J, Sherman MA, Waring A, Lehrer RI.