General Information

    • DRAMP ID

    • DRAMP01648

    • Peptide Name

    • Dermaseptin-like PBN2 (DRP-PBN2; Plasticin-B1a; Frogs, amphibians, animals)

    • Source

    • Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GLVTSLIKGAGKLLGGLFGSVTGGQS

    • Sequence Length

    • 26

    • Protein Existence

    • Homology

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-negative bacteria: Escherichia coli B (MIC=1.5 µM), Salmonella typhimurium (MIC=3.1 µM), Salmonella enteritidis (MIC=1.5 µM), Enterobacter cloacae (MIC=12.5 µM), Klebsiella pneumoniae (MIC=0.8 µM);
      • Gram-positive bacteria: Aerococcus viridans (MIC=3.1 µM), Bacillus megaterium (MIC=0.8 µM), Staphylococcus aureus (MIC=3.1 µM), Staphylococcus haemolyticus (MIC=0.8 µM).
      • Fungi: Saccaromyces cerevisiae (MIC=3.1 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

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP01648 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

Physicochemical Information

    • Formula

    • C108H185N29O33

    • Absent Amino Acids

    • CDEHMNPRWY

    • Common Amino Acids

    • G

    • Mass

    • 2417.83

    • PI

    • 10

    • Basic Residues

    • 2

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 10

    • Net Charge

    • +2

    • Boman Index

    • 17.93

    • Hydrophobicity

    • 0.7

    • Aliphatic Index

    • 116.15

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 13

DRAMP01648

DRAMP01648 chydropathy plot

Comments Information

    • Function

    • Possesses a potent antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and fungi. Probably acts by disturbing membrane functions with its amphipathic structure.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain.

    • Reference

    • Eur J Biochem. 2003 May;270(9):2068-2081.

    • Author

    • Vanhoye D, Bruston F, Nicolas P, Amiche M.
  • ·Literature 2

    • Title

    • Membrane association, electrostatic sequestration, and cytotoxicity of Gly-Leu-rich peptide orthologs with differing functions.

    • Reference

    • Biochemistry. 2004 Jul 6;43(26):8391-8409.

    • Author

    • Vanhoye D, Bruston F, El Amri S, Ladram A, Amiche M, Nicolas P.