General Information
-
DRAMP ID
- DRAMP18621
-
Peptide Name
- Temporin-PEa (Temporin-PE peptide derivative)
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Source
- Synthetic construct
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Family
- Derived from the peptide Temporin-PE
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Gene
- Not found
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Sequence
- FLYIVAKLLSGLL
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Sequence Length
- 13
-
UniProt Entry
- No entry found
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Protein Existence
- Synthetic
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anitifungal
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Target Organism
-
- [Ref.29191658]Gram-positive bacteria: Staphylococcus aureus (MIC=1.0 μM), Methicillin-resistant Staphylococcus aureus (MIC=2.0 μM), Enterococcus faecalis (MIC=2.0 μM);
- Fungus: Candida albicans (MIC=2.0 μM).
- Cancer cell lines: NCI-H157 (IC50=3.398 μM), U251MG (IC50=3.520 μM), PC-3 (IC50=27.62 μM), MDA-MB-435s (IC50=9.864 μM), HMEC-1 (IC50=40.30 μM).
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Hemolytic Activity
-
- [Ref.29191658]HC50=531.7 μM against horse 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
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP18621.
Physicochemical Information
-
Formula
- C73H120N14O16
Absent Amino Acids
- CDEHMNPQRTW
Common Amino Acids
- L
Mass
- 1449.84
PI
- 8.59
Basic Residues
- 1
Acidic Residues
- 0
Hydrophobic Residues
- 9
Net Charge
- +1
-
Boman Index
- 3020
Hydrophobicity
- 1.992
Aliphatic Index
- 210
Half Life
-
- Mammalian:1.1 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 1490
Absorbance 280nm
- 124.17
Polar Residues
- 3
DRAMP18621
Comments Information
Function
- Antimicrobial activity against Gram-positive bacteria and fungi. Weak hemolytic activity.
Literature Information
- ·Literature 1
-
Title
- Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus.
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Pubmed ID
- 29191658
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Reference
- Biochem Biophys Res Commun. 2018 Jan 22;495(4):2539-2546.
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Author
- Sang M, Wu Q, Xi X, Ma C, Wang L, Zhou M, Burrows JF, Chen T.