• DRAMP ID

    • DRAMP01649
    • Peptide Name

    • Dermaseptin-BI (Dermaseptin B1; Frogs, amphibians, animals)
    • Source

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

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

    • Not found
    • Sequence

    • AMWKDVLKKIGTVALHAGKAALGAVADTISQ
    • Sequence Length

    • 31
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=15 µg/ml);
      • Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=30 µg/ml).
      • Fungi: Tricophyton rubrum (IP 1400-82) (MIC=15 µg/ml), Microsporum canis (IP 1194) (MIC=10µg/ml), Arthroderma simii (IP 1063-74) (MIC=30 µg/ml), Cryptococcus neoformans (IP 960-67) (MIC=15 µg/ml), Cryptococcus neofonnans (IP 962-67) (MIC=15 µg/ml), Aspergillus fumigatus (IP 1025-70)(MIC=125 µg/ml), Aerornonas caviae (IP 67-16 T) (MIC=60 µg/ml), Candida albicans (IP 884-65) (MIC=15 µg/ml).
    • 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
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01649 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C142H239N39O40S
    • Absent Amino Acids

    • CEFNPRY
    • Common Amino Acids

    • A
    • Mass

    • 3164.76
    • PI

    • 9.53
    • Basic Residues

    • 5
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 16
    • Net Charge

    • +3
    • Boman Index

    • -1.49
    • Hydrophobicity

    • 0.448
    • Aliphatic Index

    • 113.55
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 183.33
    • Polar Residues

    • 6

DRAMP01649

DRAMP01649 chydropathy plot
    • Function

    • Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure.
    • Tissue specificity

    • Expressed by the skin glands.
    • PTM

    • C-terminal amidation (Potential).
  • ·Literature 1
    • Title

    • Isolation and structure of novel defensive peptides from frog skin.
    • Reference

    • Eur J Biochem. 1994 Jan 15;219(1-2):145-154.
    • Author

    • Mor A, Nicolas P.
  • ·Literature 2
    • Title

    • Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins.
    • Reference

    • J Biol Chem. 1994 Jul 8;269(27):17847-17852.
    • Author

    • Amiche M, Ducancel F, Mor A, Boulain JC, Menez A, Nicolas P.