General Information
-
DRAMP ID
- DRAMP18536
-
Peptide Name
- A20L (V13KL peptide derivative)
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Source
- Synthetic construct
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Family
- Derived from the framework peptide V13KL
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Gene
- Not found
-
Sequence
- KWKSFLKTFKSAKKTVLHTLLKAISS
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Sequence Length
- 26
-
UniProt Entry
- No entry found
-
Protein Existence
- Synthetic
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram-
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Target Organism
-
- [Ref.17158938]Gram-negative bacteria: Pseudomonas aeruginosa PAO1(MIC=7.8 μg/ml), Pseudomonas aeruginosa WR5 (MIC=31.3 μg/ml), Pseudomonas aeruginosa PAK (MIC=31.3 μg/ml), Pseudomonas aeruginosa PA14 (MIC=15.6 μg/ml), Pseudomonas aeruginosa M2 (MIC=15.6 μg/ml), Pseudomonas aeruginosa CP204 (MIC=7.7 μg/ml), The geometric mean of MIC values above six Gram-negative strains (MIC=15.6 μg/ml)
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Hemolytic Activity
-
- [Ref.17158938]MHC=31.3 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
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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 DRAMP18536.
Physicochemical Information
-
Formula
- C142H236N36O34
Absent Amino Acids
- CDEGMNPQRY
Common Amino Acids
- K
Mass
- 2991.66
PI
- 10.78
Basic Residues
- 8
Acidic Residues
- 0
Hydrophobic Residues
- 11
Net Charge
- +8
-
Boman Index
- -2427
Hydrophobicity
- -0.139
Aliphatic Index
- 93.85
Half Life
-
- Mammalian:1.3 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 5500
Absorbance 280nm
- 220
Polar Residues
- 7
DRAMP18536

Comments Information
Function
- Antibacterial activity against Gram-negative bacteria. Leucine to replace Alanine at the position 20 on the peptide V13KL. Has hemolytic activity.
Literature Information
- ·Literature 1
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Title
- Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides.
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Pubmed ID
- 17158938
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Reference
- Antimicrob Agents Chemother. 2007 Apr;51(4):1398-406.
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Author
- Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS.