• DRAMP ID

    • DRAMP21223
    • Peptide Name

    • IsCT-p (Derived from IsCT-P)
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • ILKKIWKpIKKLF
    • Sequence Length

    • 13
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic form
    • Biological Activity

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

      • [Ref.16040002] Gram-positive bacteria : Staphylococcus aureus(KCTC 1621)(MIC=1 μM), MRSA (CCARM 3001)(MIC=2 μM), MRSA (CCARM 3543)(MIC=1 μM), Bacillus subtilis(KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=1 μM);
      • Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=2 μM), MDRPA (CCARM 2095)(MIC=2 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM)
    • Hemolytic Activity

      • [Ref.16040002] 0% hemolysis at 200 μM against human red blood cells
    • Cytotoxicity

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

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • Mixed(D-Pro8)
    • Structure

    • Random coil
    • Structure Description

    • This result indicated that D-Pro in the central position of a short a-helical peptide provides more remarkable structural flexibility than L-Pro.
    • Helical Wheel Diagram

    • DRAMP21223 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP21223.
    • Formula

    • C80H134N18O12
    • Absent Amino Acids

    • ACDEGHMNPQRSTVY
    • Common Amino Acids

    • K
    • Mass

    • 1655.19
    • PI

    • 10.6
    • Basic Residues

    • 5
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +5
    • Boman Index

    • 216
    • Hydrophobicity

    • 0.269
    • Aliphatic Index

    • 150
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 458.33
    • Polar Residues

    • 0

DRAMP21223

    • Function

    • Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria
  • ·Literature 1
    • Title

    • The role of the central L- or D-Pro residue on structure and mode of action of a cell-selective alpha-helical IsCT-derived antimicrobial peptide.
    • Reference

    • Biochem Biophys Res Commun. 2005 Sep 9;334(4):1329-35.
    • Author

    • Lim SS, Kim Y, Park Y, Kim JI, Park IS, Hahm KS, Shin SY