• DRAMP ID

    • DRAMP21280
    • Peptide Name

    • LK-L8K (Derived from LK)
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • LKKLLKLKKKLLKLAG
    • Sequence Length

    • 16
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic form
    • Biological Activity

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

      • [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC>40 μM);
      • Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM)
    • Hemolytic Activity

      • [Ref.23894079] MHC10=160 μM against human red blood cells
    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP21280 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP21280.
    • Formula

    • C89H171N23O17
    • Absent Amino Acids

    • CDEFHIMNPQRSTVWY
    • Common Amino Acids

    • KL
    • Mass

    • 1835.48
    • PI

    • 10.78
    • Basic Residues

    • 7
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 8
    • Net Charge

    • +7
    • Boman Index

    • -166
    • Hydrophobicity

    • 0.044
    • Aliphatic Index

    • 176.88
    • Half Life

      • Mammalian:5.5 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 1

DRAMP21280

    • Function

    • Antibacterial activity against Gram-negative bacteria. Uncertain antibacterial activity against Gram-positive bacteria.
  • ·Literature 1
    • Title

    • Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides.
    • Reference

    • ChemMedChem. 2013 Oct;8(10):1638-42. doi: 10.1002/cmdc.201300264.
    • Author

    • Son M, Lee Y, Hwang H, Hyun S, Yu J