• DRAMP ID

    • DRAMP03683
    • Peptide Name

    • Vespid chemotactic peptide 5g (VCP 5g; Insects, animals)
    • Source

    • Vespa magnifica
    • Family

    • Belongs to the MCD family (Crabrolin subfamily)
    • Gene

    • Not found
    • Sequence

    • FLIIRRPIVLGLL
    • Sequence Length

    • 13
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.16330062]Gram-negative bacterium: Escherichia coli ATCC 25922 (MIC=30 µg/ml);
      • Gram-positive bacterium: Staphylococcus aureus ATCC 2592 (MIC=10 µg/ml);
      • Yeast: Candida albicans ATCC 2002 (MIC=12.5 µg/ml).
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Not found
    • 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

    • DRAMP03683 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP03683.
    • Formula

    • C75H131N19O14
    • Absent Amino Acids

    • ACDEHKMNQSTWY
    • Common Amino Acids

    • L
    • Mass

    • 1522.98
    • PI

    • 12
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +2
    • Boman Index

    • 12.56
    • Hydrophobicity

    • 1.9
    • Aliphatic Index

    • 232.31
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 1

DRAMP03683

    • Function

    • Mast cell degranulating peptide (By similarity). Has little hemolytic activity. Shows antimicrobial activity against the Gram-negative bacteria and the Gram-positive bacteria. Also has antifungal activity.
    • Tissue specificity

    • Expressed by the venom gland.
    • PTM

    • C-terminal amidation (By similarity).
  • ·Literature 1
    • Title

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

    • Toxicon. 2006 Feb;47(2):249-53.
    • Author

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