• DRAMP ID

    • DRAMP01938
    • Peptide Name

    • CPRF-Eb (caerulein precursor-related fragment; Frogs, amphibians, animals)
    • Source

    • Rana esculenta complex
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • GLGSFLKNAIKIAGKVGSTIGKVADAIGNKE
    • Sequence Length

    • 31
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

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

      • Gram-negative bacterium: Escherichia coli (MIC=5 µM).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • 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

    • DRAMP01938 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01938.
    • Formula

    • C136H234N38O41
    • Absent Amino Acids

    • CHMPQRWY
    • Common Amino Acids

    • G
    • Mass

    • 3057.58
    • PI

    • 9.83
    • Basic Residues

    • 5
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 13
    • Net Charge

    • +3
    • Boman Index

    • -12.47
    • Hydrophobicity

    • 0.187
    • Aliphatic Index

    • 107.1
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 11

DRAMP01938

DRAMP01938 chydropathy plot
    • Function

    • Potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli. No peptide, at concentrations up to 100 µM, inhibited the growth of the fungal pathogen C. albicans.
    • Sequence similarity

    • This peptide shows limited amino acid sequence similarity to the homologous exon gene products that encode the N-terminal flanking peptides of preprocaerulein, preproxenopsin, and preprolevitide.
  • ·Literature 1
    • Title

    • Characterization of novel antimicrobial peptides from the skins of frogs of the Rana esculenta complex.
    • Reference

    • Peptides. 2003 Jul;24(7):955-961.
    • Author

    • Ali MF, Knoop FC, Vaudry H, Conlon JM.