General Information

    • DRAMP ID

    • DRAMP01935

    • Peptide Name

    • Brevinin-2Ej (Frogs, amphibians, animals)

    • Source

    • Rana esculenta complex

    • Family

    • Belongs to the frog skin active peptide family (Brevinin subfamily)

    • Gene

    • Not found

    • Sequence

    • GIFLDKLKNFAKGVAQSLLNKASCKLSGQC

    • Sequence Length

    • 30

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Not found

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-

    • Target Organism

      • Gram-negative bacterium: Escherichia coli (MIC=2 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

Structure Information

    • 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

    • DRAMP01935 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

Physicochemical Information

    • Formula

    • C141H237N39O40S2

    • Absent Amino Acids

    • EHMPRTWY

    • Common Amino Acids

    • KL

    • Mass

    • 3182.79

    • PI

    • 9.6

    • Basic Residues

    • 5

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 12

    • Net Charge

    • +4

    • Boman Index

    • -20.7

    • Hydrophobicity

    • 0.103

    • Aliphatic Index

    • 97.67

    • Half Life

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

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 4.31

    • Polar Residues

    • 10

DRAMP01935

DRAMP01935 chydropathy plot

Comments Information

    • 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 Information

  • ·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.