• DRAMP ID

    • DRAMP21305
    • Peptide Name

    • R8 (De novo synthesis)
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • RRRRRRRR
    • Sequence Length

    • 8
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic form
    • Biological Activity

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

      • [Ref.23085001] Gram-positive bacteria : Staphylococcus aureus(ATCC 33591)(MIC=44 μM);
      • Gram-negative bacteria : Escherichia coli(ATCC 25922)(MIC=44 μM)
    • Hemolytic Activity

      • [Ref.23085001] HC50>128 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

    • L
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP21305 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP21305.
    • Formula

    • C48H98N32O9
    • Absent Amino Acids

    • ACDEFGHIKLMNPQSTV
    • Common Amino Acids

    • R
    • Mass

    • 1267.52
    • PI

    • 12.85
    • Basic Residues

    • 8
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 0
    • Net Charge

    • +8
    • Boman Index

    • -11936
    • Hydrophobicity

    • -4.5
    • Aliphatic Index

    • 0
    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 0

DRAMP21305

    • Function

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

    • Antimicrobial and cell-penetrating properties of penetratin analogs: effect of sequence and secondary structure.
    • Reference

    • Biochim Biophys Acta. 2013 Feb;1828(2):223-32. doi: 10.1016/j.bbamem.2012.10.010.
    • Author

    • Bahnsen JS, Franzyk H, Sandberg-Schaal A, Nielsen HM