• DRAMP ID

    • DRAMP02934
    • Peptide Name

    • PM1-S (linear derivative of PM1)
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • RRWSFRVSYRGFSYRKSR
    • Sequence Length

    • 18
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli UB1005 (MIC=4 µg/ml), E. coli DC2 (MIC=4 µg/ml), Salmonella typhimurium (defensin-sensitive) (MIC=2 µg/ml), S. typhimurium (MIC=8 µg/ml), Pseudomonas aeruginosa K799 (MIC=32 µg/ml), P. aeruginosa Z61 (MIC=16 µg/ml);
      • Gram-positive bacteria: Staphylococcus aureus SAP0017 (MIC=32 µg/ml), Staphylococcus epidermidis (MIC=16 µg/ml), Enterococcus faecalis (MIC=2 µg/ml).
      • Yeasy: Candida albicans (MIC=64 µg/ml).
    • Hemolytic Activity

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

    • No secondary structure (CD)
    • Structure Description

    • The CD spectra of PM1-S indicates that, in all environments (phosphate buffer, TFE, and liposomes), the peptide displays no observable patterns that could be related to structural features. This indicates that PM1-S is a flexible molecule with no favoured conformation.
    • Helical Wheel Diagram

    • DRAMP02934 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C108H164N38O25
    • Absent Amino Acids

    • ACDEHILMNPQT
    • Common Amino Acids

    • R
    • Mass

    • 2394.73
    • PI

    • 12.01
    • Basic Residues

    • 7
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 4
    • Net Charge

    • +7
    • Boman Index

    • -95.68
    • Hydrophobicity

    • -1.567
    • Aliphatic Index

    • 16.11
    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 8480
    • Absorbance 280nm

    • 498.82
    • Polar Residues

    • 7

DRAMP02934

DRAMP02934 chydropathy plot
    • Function

    • PM1-S remaines active against Gram-negative bacteria but displayed poor activity to both Gram-positive and fungal microorganisms.
  • ·Literature 1
    • Title

    • Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I.
    • Reference

    • Biochim Biophys Acta. 2004 May 6;1698(2):239-250.
    • Author

    • Powers JP, Rozek A, Hancock RE.