• DRAMP ID

    • DRAMP01668
    • Peptide Name

    • Dermaseptin-1 (DS I; Dermaseptin-S1, DS1; Frogs, amphibians, animals)
    • Source

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

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

    • Not found
    • Sequence

    • ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ
    • Sequence Length

    • 34
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Fungi: Microsporum canis (IP 1194) (MIC=50 µg/ml), Tricophyton rubrum (IP 1400-82) (MIC=100 µg/ml), Arthroderma simii (IP 1063-74) (MIC=100 µg/ml), Aspergillus fumigatus (IP 1025-70) (MIC=100 µg/ml), Aerornonas caviae IP (67-16) T (MIC=50 µg/ml), Cryptococcus neoformans (IP 960-67) (MIC=15 µg/ml), Cryptococcus neoformans (IP 962-67) (MIC=15 µg/ml), Candida albicans (IP 884-65) (MIC=60 µg/ml);
      • Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=5 µg/ml);
      • Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=200 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

    • Cell membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Alpha helix (CD)
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01668 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C152H257N43O44S2
    • Absent Amino Acids

    • CEFNPRVY
    • Common Amino Acids

    • A
    • Mass

    • 3455.09
    • PI

    • 10
    • Basic Residues

    • 5
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 15
    • Net Charge

    • +4
    • Boman Index

    • -5.55
    • Hydrophobicity

    • 0.185
    • Aliphatic Index

    • 92.35
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 166.67
    • Polar Residues

    • 9

DRAMP01668

DRAMP01668 chydropathy plot
    • Function

    • Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. This peptide could also inhibit HIV infection at a concentration that is also toxic to T cells (J Virol 2005; 79
    • Tissue specificity

    • Expressed by the skin glands.
  • ·Literature 1
    • Title

    • Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.
    • Reference

    • Biochemistry. 1991 Sep 10;30(36):8824-8830.
    • Author

    • Mor A, Nguyen VH, Delfour A, Migliore-Samour D, Nicolas P.
  • ·Literature 2
    • 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.