• DRAMP ID

    • DRAMP01842
    • Peptide Name

    • Ascaphin-3 (Frogs, amphibians, animals)
    • Source

    • Ascaphus truei (Coastal tailed frog)
    • Family

    • Belongs to the ascaphin family
    • Gene

    • Not found
    • Sequence

    • GFRDVLKGAAKAFVKTVAGHIANI
    • Sequence Length

    • 24
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.15207717]Gram-negative bacterium: Escherichia coli (MIC=6 µM);
      • Gram-positive bacterium: Staphylococcus aureus (MIC>50 µM).
    • Hemolytic Activity

      • [Ref.15207717]HC50>200 μM against human erythrocytes
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • 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

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01842 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C114H187N33O29
    • Absent Amino Acids

    • CEMPQSWY
    • Common Amino Acids

    • A
    • Mass

    • 2483.94
    • PI

    • 10.29
    • Basic Residues

    • 5
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 13
    • Net Charge

    • +4
    • Boman Index

    • -9.45
    • Hydrophobicity

    • 0.488
    • Aliphatic Index

    • 105.83
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 5

DRAMP01842

DRAMP01842 chydropathy plot
    • Function

    • Antimicrobial peptide that shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Has a very weak hemolytic activity. Tissue specificity
  • ·Literature 1
    • Title

    • The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei.
    • Reference

    • Biochem Biophys Res Commun. 2004 Jul 16;320(1):170-175.
    • Author

    • Conlon JM, Sonnevend A, Davidson C, Smith DD, Nielsen PF.