General Information
-
DRAMP ID
- DRAMP03743
-
Peptide Name
- Androctonin (Arthropods, animals)
-
Source
- Androctonus australis (Sahara scorpion)
-
Family
- Not found
-
Gene
- Not found
-
Sequence
- RSVCRQIKICRRRGGCYYKCTNRPY
-
Sequence Length
- 25
-
UniProt Entry
- P56684
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
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Target Organism
-
- [Ref.10942757] Gram-positive bacteria: Micrococcus luteus (MIC=0.6-1.5 μM), Aerococcus viridans (MIC=0.3-0.6 μM), Staphylococcus aureus (MIC=15-30 μM);
- Gram-negative bacteria: Escherichia coli D31 (MIC=3-6 μM), Escherichia coli D22 (MIC=6-15 μM), Escherichia coli 1106 (MIC=6-15 μM), Salmonella typhimurium (MIC=3-6 μM).
- Fungi: Alternaria brassicola (MIC=3-6 μM), Fusarium culmorum (MIC=3-6 μM), Fusarium oxysporum (MIC=6-12 μM), Neurospora crassa (MIC=6-12 μM), Nectria haematococca (MIC=6-12 μM), Trichoderma viridae (MIC=6-12 μM);
- Yeast: Candida albicans (MIC=1.6-3.15 μM).
- [Ref.8939880] Gram-positive bacteria: Bacillus subtilis (MIC=1.5-3.0 μM);
- Gram-negative bacteria: Escherichia coli D22 (MIC>30 μM), Pseudomonas syringae (MIC=1.5-3.0 μM), Pseudomonas syringae pv.syringae (MIC=15-22 μM), Pseudomonas syringae phaseoli (MIC=1.5-3.0 μM), Pseudomonas syringae pv.pisi (MIC=6-15 μM), Pseudomonas syringae pv. maculicola (MIC=3-6 μM), Phoma valerianella (MIC=15-22 μM), Xanthomonas compestris pv.compestris (MIC=3-6 μM), Xanthomonas vesicatoria 687.3 (MIC=1.5-3.0 μM), Xanthomonas vesicatoria B229RI (MIC=1.5-3.0 μM);
- Fungi: Alternaria dauci (MIC=8-16 μM), Stemphylium (MIC=4-8 μM), Fusarium oxysporum M. (MIC=2-4 μM), Fusarium oxysporum L. (MIC=2-4 μM), Botrytis cinerea (MIC=6-12 μM), B. petunia (MIC=4-8 μM), Verticilium toreilis (MIC=2-4 μM), Aspergillus fumigatus (MIC=25-50 μM).
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Hemolytic Activity
-
- [Ref.8939880] It exhibits no hemolytic activity on porcine or bovine erythrocytes at a concentration of up to 150 μM.
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
- Cell membrane
Structure Information
-
Linear/Cyclic
- Cyclic
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- Disulfide bond between Cys4 and Cys20,Cys10 and Cys16.
-
Stereochemistry
- L
-
Structure
- Beta strand (2 strands; 8 residues)
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Structure Description
- The structure of androctonin involves a well-defined highly twisted anti-parallel beta-sheet with strands connected by a more variable positively charged turn.
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Helical Wheel Diagram
-
PDB ID
- 1CZ6 resolved by NMR.
- 1CZ6-> 
-
Predicted Structure
- There is no predicted structure for DRAMP03743.
Physicochemical Information
-
Formula
- C129H215N47O33S4
Absent Amino Acids
- ADEFHLMW
Common Amino Acids
- R
Mass
- 3080.66
PI
- 10.22
Basic Residues
- 8
Acidic Residues
- 0
Hydrophobic Residues
- 3
Net Charge
- +8
-
Boman Index
- -98.31
Hydrophobicity
- -1.056
Aliphatic Index
- 42.8
Half Life
-
- Mammalian:1 hour
- Yeast:2 min
- E.coli:2 min
Extinction Coefficient Cystines
- 4720
Absorbance 280nm
- 196.67
Polar Residues
- 12
DRAMP03743
Comments Information
Function
- Androctonin is a highly cationic antimicrobial peptide from scorpion exhibiting a broad spectrum of activities against bacteria (Gram-positive and Gram-negative) and filamentous fungi. Acts on the membrane of the bacterial cells. It destabilize a membrane by modifying its properties.
PTM
- Contains two disulfide bonds 4-20; 10-16.
Literature Information
- ·Literature 1
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Title
- Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood.
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Pubmed ID
- 8939880
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Reference
- J Biol Chem. 1996 Nov 22;271(47):29537-29544.
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Author
- Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann JA, van Dorsselaer A, Bulet P.
- ·Literature 2
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Title
- Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer.
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Pubmed ID
- 10563585
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Reference
- J Biomol Struct Dyn. 1999 Oct;17(2):367-380.
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Author
- Mandard N, Sy D, Maufrais C, Bonmatin JM, Bulet P, Hetru C, Vovelle F.
- ·Literature 3
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Title
- Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family.
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Pubmed ID
- 10942757
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Reference
- J Biol Chem. 2000 Oct 27;275(43):33464-70.
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Author
- Silva PI Jr, Daffre S, Bulet P.