• DRAMP ID

    • DRAMP01164
    • Peptide Name

    • Bombinin (toads, amphibians, animals)
    • Source

    • Bombina variegata (Yellow-bellied toad)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • GIGALSAKGALKGLAKGLAEHFAN
    • Sequence Length

    • 24
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.8223491]Gram-negative bacterium: Escherichia coli D21 (MIC=3 µM);
      • Gram-positive bacterium: Staphylococcus aureus Cowan 1 (MIC=14 µM).
    • Hemolytic Activity

      • [Ref.8223491] The lethal concentration (LC, the lowest concentration that inhibits growth) was over 50 μM
    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01164 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01164.
    • Formula

    • C103H172N30O29
    • Absent Amino Acids

    • CDMPQRTVWY
    • Common Amino Acids

    • A
    • Mass

    • 2294.68
    • PI

    • 9.7
    • Basic Residues

    • 4
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 12
    • Net Charge

    • +3
    • Boman Index

    • 4.98
    • Hydrophobicity

    • 0.358
    • Aliphatic Index

    • 106.25
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 7

DRAMP01164

DRAMP01164 chydropathy plot
    • Function

    • Has antimicrobial and hemolytic activities.
    • Tissue specificity

    • Expressed by the skin glands.
    • PTM

    • C-terminal amidation.
    • Caution

    • Residue 20 is assigned as E by similarity to other bombin sequences instead of Z (Glutamic acid or Gutamine) given
  • ·Literature 1
    • Title

    • Isolation and structural resolution of a haemolytically active polypeptide from the immune secretion of a European toad.
    • Reference

    • Monatsh. Chem. 1970;101:182-189.
    • Author

    • Csordas A, Michl H.
  • ·Literature 2
    • Title

    • Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata.
    • Reference

    • EMBO J. 1993; 12:4829-4832.
    • Author

    • Mignogna G, Simmaco M, Kreil G, Barra D.