• DRAMP ID

    • DRAMP03573
    • Peptide Name

    • LL-37(13-37)(C-terminal fragment of LL-37; Human, mammals, animals)
    • Source

    • Homo sapiens (Human)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • IGKEFKRIVQRIKDFLRNLVPRTES
    • Sequence Length

    • 25
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacterium: Escherichia coli K12 (MIC=80 µM).
      • Drug-resistant KBv cancer cells (LC50=39 µM), Drug-sensitive KB cancer cells (LC50=40 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

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bonds
    • Stereochemistry

    • L
    • Structure

    • Alpha helix (1 helices; 14 residues)
    • Structure Description

    • Residues 17-29 of LL-37(13-37) are helical.
    • Helical Wheel Diagram

    • DRAMP03573 helical wheel diagram
    • PDB ID

    • 2FCG resolved by NMR.
    • Predicted Structure

    • There is no predicted structure for DRAMP03573.
    • Formula

    • C137H232N42O36
    • Absent Amino Acids

    • ACHMWY
    • Common Amino Acids

    • R
    • Mass

    • 3043.61
    • PI

    • 10.93
    • Basic Residues

    • 7
    • Acidic Residues

    • 3
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +4
    • Boman Index

    • -77.24
    • Hydrophobicity

    • -0.624
    • Aliphatic Index

    • 101.2
    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP03573

DRAMP03573 chydropathy plot
    • The slightly lower activity of LL-37(13-37) may result from the interference of the disordered regions with membrane binding of the peptide.

  • ·Literature 1
    • Title

    • Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region.
    • Reference

    • J Am Chem Soc. 2006 May 3;128(17):5776-5785.
    • Author

    • Li X, Li Y, Han H, Miller DW, Wang G.