General Information

    • DRAMP ID

    • DRAMP02844

    • Peptide Name

    • CP10A (Indolicidin peptide derivative; mammals, animals)

    • Source

    • Bos taurus (Bovine)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • ILAWKWAWWAWRR

    • Sequence Length

    • 13

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

      • Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=4 µg/ml), S. aureus SAP0017 MRSA (MIC=4 µg/ml), Staphylococcus haemolyticus Clinical isolate (MIC=2 µg/ml), S. haemolyticus Vancomycin-resistant isolate (MIC=1 µg/ml), Staphylococcus epidermidis Clinical isolate (MIC=2 µg/ml), Enterococcus faecalis ATCC 29212 (MIC=8 µg/ml), Listeria monocytogenes NCTC 7973 (MIC=1 µg/ml), Streptococcus pyogenes ATCC 19615 (MIC=1 µg/ml), Corynebacterium xerosis Lab strain (MIC=1 µg/ml).(Ref.2)

    • 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

    • Alpha helix (1 helices; 8 residues)

    • Structure Description

    • The structure of CP10A in DPC micelles determined from NMR data is mainly a-helical with elements of 310 helical geometry.

    • Helical Wheel Diagram

    • DRAMP02844 helical wheel diagram

    • PDB ID

    • 1HR1 resolved by NMR.
  • 1HR1-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP02844.

Physicochemical Information

    • Formula

    • C94H125N25O14

    • Absent Amino Acids

    • CDEFGHMNPQSTVY

    • Common Amino Acids

    • W

    • Mass

    • 1829.19

    • PI

    • 12.01

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 10

    • Net Charge

    • +3

    • Boman Index

    • -8.47

    • Hydrophobicity

    • -0.285

    • Aliphatic Index

    • 83.08

    • Half Life

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

    • Extinction Coefficient Cystines

    • 27500

    • Absorbance 280nm

    • 2291.67

    • Polar Residues

    • 0

DRAMP02844

Comments Information

    • Function

    • A derivative of indolicidin, CP10A, has alanine residues substituted for proline residues and has improved activity against Gram-positive organisms.

    • Chemical modification

    • C-terminal amidation.

Literature Information

  • ·Literature 1

    • Title

    • Salt-resistant alpha-helical cationic antimicrobial peptides.

    • Reference

    • Antimicrob. Agents Chemother. 1999,43:1542-1548.

    • Author

    • Friedrich, C, M. G. Scott, N. Karunaratne, H. Yan, and R. E. Hancock.