• DRAMP ID

    • DRAMP03217
    • Peptide Name

    • M-oxotoxin-Ot1a (Oxyopinin-1, Oxki1; spiders, Arthropods, animals)
    • Source

    • Oxyopes takobius (Lynx spider) (Oxyopes foliiformis)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • FRGLAKLLKIGLKSFARVLKKVLPKAAKAGKALAKSMADENAIRQQNQ
    • Sequence Length

    • 48
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.11976325]Gram-negative bacterium: Escherichia coli (MIC=1.6 µM);
      • Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus (MIC=6.2 µM).
    • Hemolytic Activity

      • [Ref.11976325]100% hemolytic activity at 50 µM against sheep red blood cells
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Cell membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP03217 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP03217.
    • Formula

    • C235H409N71O60S
    • Absent Amino Acids

    • CHTWY
    • Common Amino Acids

    • AK
    • Mass

    • 5221.33
    • PI

    • 11.26
    • Basic Residues

    • 12
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 22
    • Net Charge

    • +10
    • Boman Index

    • -67.16
    • Hydrophobicity

    • -0.204
    • Aliphatic Index

    • 103.96
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 7

DRAMP03217

DRAMP03217 chydropathy plot
    • Function

    • Disrupts cell membranes, particularly those rich in phosphocholine, through formation of pores. Has antimicrobial activity against Gram-negative bacterium E. coli, Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep erythrocytes. Has insecticidal activity against S. frugiperda ovarian cells by opening non-selective ion channels. Enhances the insecticidal activity of spider venom neurotoxic peptides.
  • ·Literature 1
    • Title

    • Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins.
    • Reference

    • J Biol Chem. 2002 Jun 28;277(26):23627-23637.
    • Author

    • Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T.
  • ·Literature 2
    • Title

    • Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size.
    • Reference

    • Biochim Biophys Acta. 2004 Aug 30;1664(2):182-188.
    • Author

    • Belokoneva OS, Satake H, Mal'tseva EL, Pal'mina NP, Villegas E, Nakajima T, Corzo G.