General Information

    • DRAMP ID

    • DRAMP03570

    • Peptide Name

    • LL-23 (Derived from LL-37)

    • Source

    • Homo sapiens (Human sweat)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • LLGDFFRKSKEKIGKEFKRIVQR

    • Sequence Length

    • 23

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-negative bacterium: Escherichia coli DC2 (MIC=9 µM);
      • Gram-positive bacteria: Staphylococcus aureus mprF (presence of carbonate) (MIC=3 µM), S. aureu mprF (absence of carbonate) (MIC=24 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

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Alpha helix (1 helices; 19 residues)

    • Structure Description

    • The Ser9 site splits the hydrophobic surface of the amphipathic helix into two domains, which explains its poor antimicrobial activity (active against only susceptible bacterial strains).

    • Helical Wheel Diagram

    • DRAMP03570 helical wheel diagram

    • PDB ID

    • 2LMF resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP03570.

Physicochemical Information

    • Formula

    • C130H216N38O32

    • Absent Amino Acids

    • ACHMNPTWY

    • Common Amino Acids

    • K

    • Mass

    • 2823.38

    • PI

    • 10.55

    • Basic Residues

    • 8

    • Acidic Residues

    • 3

    • Hydrophobic Residues

    • 8

    • Net Charge

    • +5

    • Boman Index

    • -69.25

    • Hydrophobicity

    • -0.844

    • Aliphatic Index

    • 80.43

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 3

DRAMP03570

DRAMP03570 chydropathy plot

Comments Information

    • Its structure, dynamics, and antimicrobial and immune modulating activities have been characterized (Biochemistry 2012).

Literature Information

  • ·Literature 1

    • Title

    • Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin.

    • Reference

    • FASEB J 2006; 20, 2068-2080.

    • Author

    • Yamasaki K et al. Gallo RL.
  • ·Literature 2

    • Title

    • Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins.

    • Reference

    • Biochemistry. 2012 Jan 17;51(2):653-664.

    • Author

    • Wang G, Elliott M, Cogen AL, Ezell EL, Gallo RL, Hancock RE.