• DRAMP ID

    • DRAMP03034
    • Peptide Name

    • Mastoparan-like peptide 12b (Insects, animals)
    • Source

    • Vespa magnifica (Hornet)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • INWKGIAAMKKLL
    • Sequence Length

    • 13
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.16330062]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=15 µg/ml);
      • Gram-positive bacteria: Staphylococcus aureus ATCC 2592 (MIC=3.7 µg/ml);
      • Fungi: Candida albicans ATCC 2002 (MIC=7.5 µg/ml).
    • Hemolytic Activity

      • [Ref.16330062]Little hemolytic activity at 50 μg/ml against rabbit red blood cells
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP03034 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C70H120N18O15S
    • Absent Amino Acids

    • CDEFHPQRSTVY
    • Common Amino Acids

    • K
    • Mass

    • 1485.89
    • PI

    • 10.3
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +3
    • Boman Index

    • 5.63
    • Hydrophobicity

    • 0.431
    • Aliphatic Index

    • 135.38
    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 458.33
    • Polar Residues

    • 2

DRAMP03034

    • Function

    • Mast cell degranulating peptide. Has little hemolytic activity. Shows antimicrobial activity.
    • Tissue specificity

    • Expressed by the venom gland.
    • PTM

    • C-terminal amidation (Leucine amide
  • ·Literature 1
    • Title

    • Two families of antimicrobial peptides from wasp (Vespa magnifica) venomThe mastoparanogen from wasp.
    • Reference

    • Toxicon. 2006 Feb;47(2):249-53. Epub 2005 Dec 5. Peptides. 2006 Dec;27(12):3053-7. Epub 2006 Oct 13.
    • Author

    • Xu X, Li J, Lu Q, Yang H, Zhang Y, Lai R.Xu X, Yang H, Yu H, Li J, Lai R.