General Information
-
DRAMP ID
- DRAMP21306
-
Peptide Name
- TL-1 (Derived from Temporin-1Tl (TL))
-
Source
- Synthetic construct
-
Family
- Not found
-
Gene
- Not found
-
Sequence
- FVQWWSKWLGRIL
-
Sequence Length
- 13
-
UniProt Entry
- No entry found
-
Protein Existence
- Synthetic form
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- [Ref.26311041] Gram-positive bacteria : Bacillus subtilis (KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis (KCTC 1917)(MIC=4 μM), Staphylococcus aureus (KCTC 1621)(MIC=2 μM);
- Gram-negative bacteria : Escherichia coli (KCTC 1682)(MIC=4 μM), Pseudomonas aeruginosa (KCTC 1637)(MIC=32 μM), Salmonella typhimurium (KCTC 1926)(MIC=4 μM)
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Hemolytic Activity
-
- [Ref.26311041] HC50=21.4 μM against human red blood cells
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Cytotoxicity
-
- [Ref.26311041] The cell viability of RAW264.7 macrophages cells induced by TL-1 is 112.2%, 109.3% and 109.3% at peptide concentrations of 2.5, 5 and 10 μM.
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Amidation
-
Nonterminal Modifications and Unusual Amino Acids
- None
-
Stereochemistry
- L
-
Structure
- Not found
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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 DRAMP21306.
Physicochemical Information
-
Formula
- C87H123N21O16
Absent Amino Acids
- ACDEHMNPTY
Common Amino Acids
- W
Mass
- 1719.06
PI
- 11
Basic Residues
- 2
Acidic Residues
- 0
Hydrophobic Residues
- 8
Net Charge
- +2
-
Boman Index
- 30
Hydrophobicity
- 0.254
Aliphatic Index
- 112.31
Half Life
-
- Mammalian:1.1 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 16500
Absorbance 280nm
- 1375
Polar Residues
- 2
DRAMP21306
Comments Information
Function
- Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria
Literature Information
- ·Literature 1
-
Title
- Enhancement of the anti-inflammatory activity of temporin-1Tl-derived antimicrobial peptides by tryptophan, arginine and lysine substitutions.
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Pubmed ID
- 26311041
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Reference
- J Pept Sci. 2015 Oct;21(10):779-85. doi: 10.1002/psc.2807.
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Author
- Rajasekaran G, Kamalakannan R, Shin SY