General Information

    • DRAMP ID

    • DRAMP02031

    • Peptide Name

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

    • Source

    • Rana dalmatina (European frog)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • ILPLLLGKVVCAITKKC

    • Sequence Length

    • 17

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Not found

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-positive bacterium: Staphylococcus aureus (MIC=7 µM);
      • Gram-negative bacterium: Escherichia coli (MIC=30 µM).

    • Hemolytic Activity

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

    • 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 (Cys11 and Cys17)

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys11 and Cys17.

    • Stereochemistry

    • L

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02031 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP02031.

Physicochemical Information

    • Formula

    • C84H154N20O19S2

    • Absent Amino Acids

    • DEFHMNQRSWY

    • Common Amino Acids

    • L

    • Mass

    • 1812.39

    • PI

    • 9.39

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +3

    • Boman Index

    • 23.69

    • Hydrophobicity

    • 1.471

    • Aliphatic Index

    • 177.65

    • Half Life

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

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 7.81

    • Polar Residues

    • 4

DRAMP02031

Comments Information

    • Sequence alignment suggests that the peptide is derived from brevinin-1 by multiple residue deletions (D for "dalmatina" and 'a' to denote the first isoform identified).

Literature Information

  • ·Literature 1

    • Title

    • An atypical member of the brevinin-1 family of antimicrobial peptides isolated from the skin of the European frog Rana dalmatina.

    • Reference

    • Comp Biochem Physiol C Toxicol Pharmacol. 2004 Feb;137(2):191-196.

    • Author

    • Conlon JM, Seidel B, Nielsen PF.