General Information

    • DRAMP ID

    • DRAMP02081

    • Peptide Name

    • Brevinin-1E (Frogs, amphibians, animals)

    • Source

    • Rana esculenta (Edible frog) (Pelophylax esculentus)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • FLPLLAGLAANFLPKIFCKITRKC

    • Sequence Length

    • 24

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Anti Mammalian Cells

    • Target Organism

      • [Ref.8163497] Gram-negative bacteria: Escherichia coliD21 (MIC=1.8 µM), Pseudomonas aeruginosa ATCC15692 (MIC=30.6 µM);
      • Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=0.4 µM), Staphylococcus aureus Cowan1 (MIC=0.6 µM);
      • Fungi: Candida albicans (MIC=4.7 µM);
      • Yeast: Saccharomyces cerevisiae (MIC=3.8 µM).

    • Hemolytic Activity

      • [Ref.8163497] LC50=0.5 µM against human red blood cell.

    • Cytotoxicity

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

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Cyclization (Cys18 and Cys24)

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys18 and Cys24.

    • Stereochemistry

    • L

    • Structure

    • Alpha helix

    • Structure Description

    • Possess an intramo-lecular disulfide bridge located at the carboxyl-terminal end.

    • Helical Wheel Diagram

    • DRAMP02081 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

Physicochemical Information

    • Formula

    • C128H209N31O27S2

    • Absent Amino Acids

    • DEHMQSVWY

    • Common Amino Acids

    • L

    • Mass

    • 2678.38

    • PI

    • 9.85

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 13

    • Net Charge

    • +4

    • Boman Index

    • 11.53

    • Hydrophobicity

    • 0.95

    • Aliphatic Index

    • 126.25

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 5.43

    • Polar Residues

    • 5

DRAMP02081

DRAMP02081 chydropathy plot

Comments Information

    • Function

    • Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and a very high hemolytic activity.

Literature Information

  • ·Literature 1

    • Title

    • Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta.

    • Reference

    • FEBS Lett. 1993 Jun 14;324(2):159-161.

    • Author

    • Simmaco M, Mignogna G, Barra D, Bossa F.
  • ·Literature 2

    • Title

    • Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.

    • Reference

    • J Biol Chem. 1994 Apr 22;269(16):11956-11961.

    • Author

    • Simmaco M, Mignogna G, Barra D, Bossa F.