• • 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

• • UniProt Entry

  • P0C022

• • Protein Existence

  • Protein level

• • 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

• • 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

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP03042.

DRAMP03042

• • 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 1

• • Title

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

• • Pubmed ID

  • 15317499

• • 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.

• • Pubmed ID

  • 11006592

• • 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).

• • Pubmed ID

  • 10775751

• • 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.