• DRAMP ID

    • DRAMP04128
    • Peptide Name

    • D5-NH2 (Derived from D0)
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • RWKRWWRRKK
    • Sequence Length

    • 10
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic
    • Biological Activity

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

      • [Ref.22518150] Gram-negative bacteria: Escherichia coli (MIC=3±0.012 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=3±0.012 µM);
      • Gram-positive bacterium: Staphylococcus aureus ATCC 25923 (MIC=6±0.012 µM).
    • Hemolytic Activity

      • [Ref.23860860] 6.5% hemolysis at 100 μM against human red blood cells
    • 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

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP04128 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP04128.
    • Formula

    • C75H116N28O11
    • Absent Amino Acids

    • ACDEFGHILMNPQSTVY
    • Common Amino Acids

    • R
    • Mass

    • 1585.93
    • PI

    • 12.48
    • Basic Residues

    • 7
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 3
    • Net Charge

    • +7
    • Boman Index

    • -69.34
    • Hydrophobicity

    • -3.24
    • Aliphatic Index

    • 0
    • Half Life

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

    • 16500
    • Absorbance 280nm

    • 1833.33
    • Polar Residues

    • 0

DRAMP04128

    • Function

    • Antibacterial activity against Gram-positive and Gram-negative bacteria.
    • Chemical modification

    • C-terminal amidation.
  • ·Literature 1
    • Title

    • The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.
    • Reference

    • Int J Microbiol. 2012;2012:764834.
    • Author

    • Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L.
  • ·Literature 2
    • Title

    • Design of Short Membrane Selective Antimicrobial Peptides Containing Tryptophan and Arginine Residues for Improved Activity, Salt-Resistance, and Biocompatibility
    • Reference

    • Biotechnol Bioeng. 2014 Jan;111(1):37-49. doi: 10.1002/bit.25003.
    • Author

    • Saravanan R, Li X, Lim K, Mohanram H, Peng L, Mishra B, Basu A, Lee JM, Bhattacharjya S, Leong SS.