• DRAMP ID

    • DRAMP03743
    • Peptide Name

    • Androctonin (Arthropods, animals)
    • Source

    • Androctonus australis (Sahara scorpion)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • RSVCRQIKICRRRGGCYYKCTNRPY
    • Sequence Length

    • 25
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
    • 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).
    • Hemolytic Activity

      • [Ref.8939880] It exhibits no hemolytic activity on porcine or bovine erythrocytes at a concentration of up to 150 μM.
    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Cell membrane
    • 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)
    • 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.
    • Helical Wheel Diagram

    • DRAMP03743 helical wheel diagram
    • PDB ID

    • 1CZ6 resolved by NMR.
  • 1CZ6-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP03743.
    • 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

DRAMP03743 chydropathy plot
    • 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 1
    • Title

    • Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood.
    • Reference

    • J Biol Chem. 1996 Nov 22;271(47):29537-29544.
    • Author

    • Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann JA, van Dorsselaer A, Bulet P.
  • ·Literature 2
    • Title

    • Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer.
    • Reference

    • J Biomol Struct Dyn. 1999 Oct;17(2):367-380.
    • Author

    • Mandard N, Sy D, Maufrais C, Bonmatin JM, Bulet P, Hetru C, Vovelle F.
  • ·Literature 3
    • 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.
    • Reference

    • J Biol Chem. 2000 Oct 27;275(43):33464-70.
    • Author

    • Silva PI Jr, Daffre S, Bulet P.