• • 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

• • 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

  • 

• • PDB ID

  • 1CZ6 resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP03743.

DRAMP03743

• • 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.

• • Pubmed ID

  • 8939880

• • 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.

• • Pubmed ID

  • 10563585

• • 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.

• • Pubmed ID

  • 10942757

• • Reference

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

• • Author

  • Silva PI Jr, Daffre S, Bulet P.