General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.