General Information

    • DRAMP ID

    • DRAMP03042

    • Peptide Name

    • Eumenine mastoparan-AF (EMP-AF; Af-113; Insects, animals)

    • Source

    • Anterhynchium flavomarginatum micado (Solitary wasp)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • INLLKIAKGIIKSL

    • Sequence Length

    • 14

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-

    • Target Organism

      • [Ref.15317499]Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MIC=5 µg/ml), S. saprophyticus CS (MIC=5 µg/ml), S. epidermidis CS (MIC=5 µg/ml), Bacillus subtilis CCT 2471 (MIC=40 µg/ml);
      • Gram-negative bacteria: Escherichia coli CCT 1371 (MIC=20 µg/ml), Escherichia coli ATCC 25922 (MIC=50 µg/ml), Pseudomonas aeruginosa ATCC 15442 (MIC=20 µg/ml).

    • Hemolytic Activity

      • [Ref.10775751]100% hemolytic activity against human erythrocytes at 10^-4 M

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Cell membrane (Note: Assumes an amphipathic alpha-helical conformation in a lipid environmen

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Alpha helix

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03042 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

Physicochemical Information

    • Formula

    • C72H134N18O17

    • Absent Amino Acids

    • CDEFHMPQRTVWY

    • Common Amino Acids

    • I

    • Mass

    • 1523.97

    • PI

    • 10.3

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 8

    • Net Charge

    • +3

    • Boman Index

    • 10.5

    • Hydrophobicity

    • 1.057

    • Aliphatic Index

    • 202.14

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 3

DRAMP03042

Comments Information

    • Function

    • Mast cell degranulating peptide. Also permeates anionic liposomes. Has hemolytic activity. Has an amphiphilic alpha-helix conformation. Shows broad-spectrum antimicrobial activity. Blocks the lobster neuromuscular transmission. Induces the depolarization of the muscle membrane.

    • Tissue specificity

    • Expressed by the venom gland.

    • PTM

    • C-terminal amidation (Leucine amide

Literature Information

  • ·Literature 1

    • Title

    • Conformation and lytic activity of eumenine mastoparan: a new antimicrobial peptide from wasp venom.

    • Reference

    • J Pept Res. 2004 Sep;64(3):95-103.

    • Author

    • dos Santos Cabrera M.P, de Souza B.M, Fontana R, Konno K, Palma M.S, de Azevedo W.F. Jr, Neto J.R.
  • ·Literature 2

    • Title

    • Advantages of using nested collision induced dissociation/post-source decay with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: sequencing of novel peptides from wasp venom.

    • Reference

    • Rapid Commun Mass Spectrom. 2000;14(19):1828-1834.

    • Author

    • Hisada M, Konno K, Itagaki Y, Naoki H, Nakajima T.
  • ·Literature 3

    • Title

    • Structure and biological activities of eumenine mastoparan-AF (EMP-AF), a new mast cell degranulating peptide in the venom of the solitary wasp (Anterhynchium flavomarginatum micado).

    • Reference

    • Toxicon. 2000 Nov;38(11):1505-1015.

    • Author

    • Konno K, Hisada M, Naoki H, Itagaki Y, Kawai N, Miwa A, Yasuhara T, Morimoto Y, Nakata Y.