General Information

    • DRAMP ID

    • DRAMP21270

    • Peptide Name

    • LK-L11A (Derived from LK)

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • LKKLLKLLKKALKLAG

    • Sequence Length

    • 16

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic form

Activity Information

    • Biological Activity

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

    • Target Organism

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

    • Hemolytic Activity

      • [Ref.23894079] MHC10=1.25 μM against human red blood cells

    • Cytotoxicity

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

    • Binding Target

    • Not found

Structure Information

    • 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

    • DRAMP21270 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP21270.

Physicochemical Information

    • Formula

    • C86H164N22O17

    • Absent Amino Acids

    • CDEFHIMNPQRSTVWY

    • Common Amino Acids

    • L

    • Mass

    • 1778.39

    • PI

    • 10.7

    • Basic Residues

    • 6

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +6

    • Boman Index

    • 570

    • Hydrophobicity

    • 0.4

    • Aliphatic Index

    • 183.13

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 1

DRAMP21270

Comments Information

    • Function

    • Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria

Literature Information

  • ·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