• DRAMP ID

    • DRAMP18482
    • Peptide Name

    • LAK120-P10
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • KKLALALKKPALLWKKLALALKKA
    • Sequence Length

    • 24
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli NCTC 9001 (MIC=0.78±0.01 μM), Escherichia coli Top 10 (MIC=0.47±0.15 μM), Pseudomonas aeruginosa (MIC=9.16±1.43 μM)
    • 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

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP18482 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP18482.
    • Formula

    • C130H233N33O25
    • Absent Amino Acids

    • CDEFGHIMNQRSTVY
    • Common Amino Acids

    • KL
    • Mass

    • 2658.49
    • PI

    • 10.85
    • Basic Residues

    • 8
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 15
    • Net Charge

    • +8
    • Boman Index

    • 815
    • Hydrophobicity

    • 0.313
    • Aliphatic Index

    • 155
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 239.13
    • Polar Residues

    • 0

DRAMP18482

DRAMP18482 chydropathy plot
    • Function

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

    • Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides.
    • Reference

    • J Biol Chem. 2012 Oct 5;287(41):34120-33.
    • Author

    • Vermeer LS, Lan Y, Abbate V, Ruh E, Bui TT, Wilkinson LJ, Kanno T, Jumagulova E, Kozlowska J, Patel J, McIntyre CA, Yam WC, Siu G, Atkinson RA, Lam JK, Bansal SS, Drake AF, Mitchell GH, Mason AJ.