General Information
-
DRAMP ID
- DRAMP03017
-
Peptide Name
- VESP-VB1 (Insects, animals)
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Source
- vespine wasps Vespa bicolor
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Family
- Not found
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Gene
- Not found
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Sequence
- FMPIIGRLMSGSL
-
Sequence Length
- 13
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UniProt Entry
- No entry found
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Protein Existence
- Not found
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
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Target Organism
-
- [Ref.18723059] Gram-negative bacterium: Escherichia coli ATCC25922(MIC=7.5μg/ml), Escherichia coli 23A(MIC=7.5μg/ml), Escherichia coli 27A(MIC=15.0μg/ml), Pseudemonas aeruginosa 3A(MIC=3.75μg/ml), Pseudemonas aeruginosa 7A(MIC=3.75μg/ml), ;
- Gram-positive bacterium: Staphylococcus aureus ATCC2592(MIC=1.9μg/ml), Staphylococcus aureus 6A(MIC=3.75μg/ml), Staphylococcus aureus 15A(MIC=1.0μg/ml);
- Fungus: Candida albicans ATCC2002(MIC=30.0μg/ml)
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Hemolytic Activity
-
- [Ref.18723059] VESP-VB1 had a little hemolytic activity of 10.2% against rabbit red blood cells, and of 3.2% against human red blood cells with peptide concentration up to 200 μg/ml
-
Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
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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 DRAMP03017.
Physicochemical Information
-
Formula
- C64H108N16O16S2
Absent Amino Acids
- ACDEHKNQTVWY
Common Amino Acids
- GILMS
Mass
- 1421.78
PI
- 9.75
Basic Residues
- 1
Acidic Residues
- 0
Hydrophobic Residues
- 5
Net Charge
- +1
-
Boman Index
- 7.52
Hydrophobicity
- 1.131
Aliphatic Index
- 120
Half Life
-
- Mammalian:1.1 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 4
DRAMP03017
Comments Information
Function
- Has antimicrobial activities against standard strains and strong antimicrobial ability against drug-resistant strains. Among the tested drug-resistant strains, Pseudemonas aeruginosa and Staphylococcus aureus were the most sensitive for this kind of antimicrobial peptide. Has a little hemolytic activity.
Literature Information
- ·Literature 1
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Title
- Antimicrobial peptides from the venoms of Vespa bicolor Fabricius.
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Pubmed ID
- 18723059
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Reference
- Peptides. 2008 Nov;29(11):1887-1892.
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Author
- Chen W, Yang X, Yang X, Zhai L, Lu Z, Liu J, Yu H.