• DRAMP ID

    • DRAMP20768
    • Peptide Name

    • Pore-forming peptide ameobapore C (EH-APP; Parasite, amoebozoa, protozoa, protists)
    • Source

    • Entamoeba histolytica
    • Family

    • Belongs to the amoebapore (amoebapore) family
    • Gene

    • Unknown
    • Sequence

    • IPVLCPVCTSLVGKLIDLVLGGAVDKVTDYLETLCAKADGLVETLCTKIVSYGIDKLIEKILEGGSAKLICGLIHAC
    • Sequence Length

    • 77
    • Evidence code

    • Protein level
    • Biological Activity

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

      • [Ref.7715451] Gram-positive bacterium: Micrococcus luteus (MIC=5 μM, MBC=10 μM)
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Alpha helix
    • Structure Description

    • Disulfide bonds at position 5-77, 8-71, 35-46
    • DRAMP20768 helical wheel diagram
    • Formula

    • C360H610N86O106S6
    • Absent Amino Acids

    • FMNQRW
    • Common Amino Acids

    • L
    • Mass

    • 8031.68
    • PI

    • 5.12
    • Basic Residues

    • 8
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 34
    • Boman Index

    • 2221
    • Hydrophobicity

    • 85.84
    • Aliphatic Index

    • 142.99
    • Half Life

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

    • 3355
    • Absorbance 280nm

    • 44.14
    • Polar Residues

    • 24

DRAMP20768

DRAMP20768 chydropathy plot
    • Function

    • Forms pores in the cytoplasmic membrane of host cells. Has antibacterial activity against M.luteus, no activity against E.coli. Implicated in the cytolytic activity of the parasite.
  • Literature 1
    • Reference

    • Mol Microbiol. 1994 Dec;14(5):895-904.
    • Author

    • Leippe M, Andrä J, Nickel R, Tannich E, Müller-Eberhard HJ.
    • Title

    • Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes.