General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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

    • There is no predicted structure for DRAMP01649.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.