General Information

    • DRAMP ID

    • DRAMP02857

    • Peptide Name

    • Indolicidin (Cathelicidin-4; mammals, animals)

    • Source

    • Bos taurus (Bovine)

    • Family

    • Belongs to the cathelicidin family

    • Gene

    • CATHL4

    • Sequence

    • ILPWKWPWWPWRR

    • Sequence Length

    • 13

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • [Ref.12074933] Gram-positive bacterium: Staphylococcus aureus (MIC=0.003%);
      • Gram-negative bacterium: Escherichia coli (MIC=0.007%);
      • Fungus: Candida albicans (MIC=0.015%)

    • 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

    • 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

    • No secondary structure

    • Structure Description

    • The backbone structure in DPC, well defined between residues 3 and 11, is extended, with two half-turns at residues Lys-5 and Trp-8. The backbone structure in SDS, well defined between residues 5 and 11, is also extended, but lackes the bend in the C-terminal half. Indolicidin in complexes with DPC has a central hydrophobic core composed of proline and tryptophan, which is bracketed by positively charged regions near the peptide termini

    • Helical Wheel Diagram

    • DRAMP02857 helical wheel diagram
  • 1G8C-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP02857.

Physicochemical Information

    • Formula

    • C100H131N25O14

    • Absent Amino Acids

    • ACDEFGHMNQSTVY

    • Common Amino Acids

    • W

    • Mass

    • 1907.3

    • PI

    • 12.01

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 7

    • Net Charge

    • +3

    • Boman Index

    • -13.9

    • Hydrophobicity

    • -1.069

    • Aliphatic Index

    • 60

    • Half Life

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

    • Extinction Coefficient Cystines

    • 27500

    • Absorbance 280nm

    • 2291.67

    • Polar Residues

    • 0

DRAMP02857

Comments Information

    • Function

    • Potent microbicidal activity; active against Staphylococcus aureus, Escherichia coli and Candida albicans.

    • Tissue specificity

    • Large granules of neutrophils.

    • PTM

    • Contains two disulfide bonds and C-terminal amidation.

Literature Information

  • ·Literature 1

    • Title

    • Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils.

    • Reference

    • J Biol Chem. 1992 Mar 5;267(7):4292-4295.

    • Author

    • Selsted ME, Novotny MJ, Morris WL, Tang YQ, Smith W, Cullor JS.
  • ·Literature 2

    • Title

    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles.

    • Reference

    • Biochemistry. 2000 Dec 26;39(51):15765-74.

    • Author

    • Rozek A, Friedrich CL, Hancock RE.
  • ·Literature 3

    • Title

    • Direct antimicrobial properties of substance P.

    • Reference

    • Life Sci. 2002 Jul 5;71(7):747-50.

    • Author

    • Kowalska K, Carr DB, Lipkowski AW.