• DRAMP ID

    • DRAMP18708
    • Peptide Name

    • Dermaseptin-S4 (DRS-S4, DS4; frog, amphibians, animals)
    • Source

    • Phyllomedusa sauvagei (Sauvage's leaf frog)
    • Family

    • Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfami
    • Gene

    • Not found
    • Sequence

    • ALWMTLLKKVLKAAAKAALNAVLVGANA
    • Sequence Length

    • 28
    • Protein Existence

    • Not found
    • Biological Activity

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

    • [Swiss_Prot Entry P80280]Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1
    • Hemolytic Activity

      • [Swiss_Prot Entry P80280]Strong hemolytic activity
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP18708 helical wheel diagram
    • PDB ID

    • 2DD6 resolved by NMR
    • Predicted Structure

    • There is no predicted structure for DRAMP18708.
    • Formula

    • C132H229N35O32S
    • Absent Amino Acids

    • CDEFHIPQRSY
    • Common Amino Acids

    • A
    • Mass

    • 2850.55
    • PI

    • 10.48
    • Basic Residues

    • 4
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 19
    • Net Charge

    • +4
    • Boman Index

    • 2550
    • Hydrophobicity

    • 1.032
    • Aliphatic Index

    • 146.79
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 203.7
    • Polar Residues

    • 4

DRAMP18708

DRAMP18708 chydropathy plot
    • Function

    • Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1. Probably acts by disturbing membrane functions with its amphipathic structure. Binds to healthy erythrocytes (this binding is receptor independent), and has strong hemolytic activity. Does not bind to P.falciparum infected erythrocytes, but accumulates within the parasite. Kills the parasite, and only at high concentrations has a hemolytic activity on the host cell.
  • ·Literature 1
    • Title

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

    • Eur. J. Biochem. 1994; 219:145-154.
    • Author

    • Mor A, Nicolas P.