• DRAMP ID

    • DRAMP03967
    • Peptide Name

    • P18 (Cecropin A(1-8)-Magainin 2(1−12) hybrid peptide analogue)
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • KWKLFKKIPKFLHLAKKF
    • Sequence Length

    • 18
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli KCTC 1682 (MIC=6.25 µM), Pseudomonas aeruginosa KCTC 1637 (MIC=1.56 µM), Proteus vulgaris (MIC=3.125 µM).
      • Gram-positive bacteria: Bacillus subtilis KCTC 1918 (MIC=0.78 µM), Staphylococcus aureus KCTC 1621 (MIC=1.56 µM), Bacillus megaterium KCTC 1096 (MIC=0.78 µM).
      • Tumor cells: MDA-MB-361 (IC50=8.0 µM), Jurkat (IC50=4.0 µM), K-562 (IC50=3.5 µM), Normal cells NIH 3T3 (IC50=75.0 µM).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Cell membrane
    • 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

    • DRAMP03967 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C118H186N28O19
    • Absent Amino Acids

    • CDEGMNQRSTVY
    • Common Amino Acids

    • K
    • Mass

    • 2300.95
    • PI

    • 10.78
    • Basic Residues

    • 8
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +8
    • Boman Index

    • -10.75
    • Hydrophobicity

    • -0.383
    • Aliphatic Index

    • 92.22
    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 323.53
    • Polar Residues

    • 0

DRAMP03967

DRAMP03967 chydropathy plot
    • MOA

    • P18 kills cancer cells by disrupting membranes (Tang C et al 2010 Org Biomol Che 8
  • ·Literature 1
    • Title

    • Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs.
    • Reference

    • J Pept Res. 2001 Dec;58(6):504-514.
    • Author

    • Shin SY, Lee SH, Yang ST, Park EJ, Lee DG, Lee MK, Eom SH, Song WK, Kim Y, Hahm KS, Kim JI.
  • ·Literature 2
    • Title

    • Antibiotic activity of reversed peptides of alpha-helical antimicrobial peptide, P18.
    • Reference

    • Protein Pept Lett. 2002 Oct;9(5):395-402.
    • Author

    • Lee SH, Lee DG, Yang ST, Kim Y, Kim JI, Hahm KS, Shin SY.