General Information
-
DRAMP ID
- DRAMP03037
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Peptide Name
- Eumenitin (Er-12; Insects, animals)
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Source
- Eumenes rubronotatus (Solitary wasp)
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Family
- Not found
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Gene
- Not found
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Sequence
- LNLKGIFKKVASLLT
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Sequence Length
- 15
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UniProt Entry
- P0C931
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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.16762455]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC>60 µM), Staphylococcus aureus ATCC 25923 (MIC=6 µM), Staphylococcus saprophytius (CS) (MIC=6 µM), Staphylococcus epidermius (CS) (MIC>60 µM), Bacillus subtilis CCT 2471 (MIC=60 µM), Bacillus thuringiensis (WT) (MIC>60 µM);
- Gram-negative bacteria: Escherichia coli CCT 1371 (MIC=6 µM), Escherichia coli ATCC 25922 (MIC=6 µM), Escherichia cloacae ATCC 23355 (MIC>60 µM), Proteus mirabilis (CS) (MIC>60 µM), Pseudomonas aeruginosa ATCC 15442 (MIC=30 µM).
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Hemolytic Activity
-
- [Ref.16762455]Non-hemolytic activity against human erythrocytes
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Cytotoxicity
-
- Not included yet
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Binding Target
- Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen
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
- 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
- Please click DRAMP03037_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C78H137N19O19
Absent Amino Acids
- CDEHMPQRWY
Common Amino Acids
- L
Mass
- 1645.06
PI
- 10.3
Basic Residues
- 3
Acidic Residues
- 0
Hydrophobic Residues
- 8
Net Charge
- +3
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Boman Index
- 5.11
Hydrophobicity
- 0.76
Aliphatic Index
- 156
Half Life
-
- Mammalian:5.5 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 4
DRAMP03037
Comments Information
Function
- Cationic linear alpha-helical antimicrobial peptide that binds preferentially to charged lipid membranes as compared with zwitterionic ones. It exhibits inhibitory activity against both Gram-positive and Gram-negative bacteria, and moderately stimulates degranulation from the rat peritoneal mast cells. Does not show hemolytic activity. May play a role in preventing infection by microorganisms during prey consumption by their larvae.
Tissue specificity
- Expressed by the venom gland.
Literature Information
- ·Literature 1
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Title
- Eumenitin, a novel antimicrobial peptide from the venom of the solitary eumenine wasp Eumenes rubronotatus.
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Pubmed ID
- 16762455
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Reference
- Peptides. 2006 Nov;27(11):2624-2631.
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Author
- Konno K, Hisada M, Naoki H, Itagaki Y, Fontana R, Rangel M, Oliveira JS, Cabrera MP, Neto JR, Hide I, Nakata Y, Yasuhara T, Nakajima T.
- ·Literature 2
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Title
- Effects of the cationic antimicrobial peptide eumenitin from the venom of solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge and pore formation activity.
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Pubmed ID
- 18206199
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Reference
- Toxicon. 2008 Apr;51(5):736-745.
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Author
- Arcisio-Miranda M, dos Santos Cabrera MP, Konno K, Rangel M, Procopio J.