• DRAMP ID

    • DRAMP03707
    • Peptide Name

    • Antimicrobial peptide 2 (AamAP2; Arthropods, animals)
    • Source

    • Androctonus amoreuxi (African fattail scorpion)
    • Family

    • Not found
    • Gene

    • ap2
    • Sequence

    • FPFSLIPHAIGGLISAIK
    • Sequence Length

    • 18
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
    • Target Organism

      • Gram-positive bacterium: Staphylococcus aureus (MIC=48 µM);
      • Gram-negative bacterium: Escherichia coli (MIC=120 µM).
      • Yeast: Candida albicans (MIC=64 µM).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Cell membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP03707 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C92H145N21O21
    • Absent Amino Acids

    • CDEMNQRTVWY
    • Common Amino Acids

    • I
    • Mass

    • 1881.29
    • PI

    • 8.76
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 10
    • Net Charge

    • +2
    • Boman Index

    • 23.97
    • Hydrophobicity

    • 1.228
    • Aliphatic Index

    • 141.11
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP03707

DRAMP03707 chydropathy plot
    • Function

    • Has antibacterial and antifungal activity. Causes hemolysis on horse erythrocytes.
    • Tissue specificity

    • Expressed by the venom gland.
    • PTM

    • C-termianal amidation.
  • ·Literature 1
    • Title

    • Antimicrobial/cytolytic peptides from the venom of the North African scorpion, Androctonus amoreuxi: biochemical and functional characterization of natural peptides and a single site-substituted analog.
    • Reference

    • Peptides. 2012 Jun;35(2):291-299.
    • Author

    • Almaaytah A, Zhou M, Wang L, Chen T, Walker B, Shaw C.