• DRAMP ID

    • DRAMP03220
    • Peptide Name

    • M-oxotoxin-Ot2c (Oxyopinin-2c, Oxki2c; spiders, Arthropods, animals)
    • Source

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

    • Belongs to the oxyopinin-2 family
    • Gene

    • Not found
    • Sequence

    • GKLSGISKVLRAIAKFFKGVGKARKQFKEASDLDKNQ
    • Sequence Length

    • 37
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Insecticidal
    • Target Organism

    • No MICs found in DRAMP database
    • Hemolytic Activity

      • [Ref.11976325]10% hemolytic activity at 50 µM against sheep red blood cells
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Cell membrane
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP03220 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP03220.
    • Formula

    • C183H308N54O50
    • Absent Amino Acids

    • CHMPTWY
    • Common Amino Acids

    • K
    • Mass

    • 4064.79
    • PI

    • 10.46
    • Basic Residues

    • 10
    • Acidic Residues

    • 3
    • Hydrophobic Residues

    • 14
    • Net Charge

    • +7
    • Boman Index

    • -73.79
    • Hydrophobicity

    • -0.562
    • Aliphatic Index

    • 79.19
    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 8

DRAMP03220

DRAMP03220 chydropathy plot
    • Function

    • Disrupts biological membranes, particularly those rich in phosphocholine. Has antimicrobial activity against Gram- negative bacterium E. coli and the Gram-positive bacteria B. subtilis and S. aureus, and hemolytic activity against sheep red blood cells. 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.