• DRAMP ID

    • DRAMP20896
    • Peptide Name

    • L9A/F10A
    • Source

    • Synthetic construct
    • Family

    • Derived from TP4
    • Gene

    • Not found
    • Sequence

    • FIHHIIGGAASAGKAIHRLIRRRRR
    • Sequence Length

    • 25
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic
    • Biological Activity

    • Antimicrobial, Antifungal
    • Target Organism

      • [Ref.29040295] Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml)
    • Hemolytic Activity

      • [Ref.29040295] 5% haemolysis at 25.00 μg/ml, 10% haemolysis at 50.00 μg/ml, 30% haemolysis at 100.00 μg/ml, 95% haemolysis at 200.00 μg/ml, 100% haemolysis at 400.00 μg/ml, 100% haemolysis at 800.00 μg/ml against mouse 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

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP20896 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP20896.
    • Formula

    • C126H216N50O27
    • Absent Amino Acids

    • CDEMNPQTVWY
    • Common Amino Acids

    • R
    • Mass

    • 2863.42
    • PI

    • 12.7
    • Basic Residues

    • 10
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 11
    • Net Charge

    • +10
    • Boman Index

    • -6989
    • Hydrophobicity

    • -0.248
    • Aliphatic Index

    • 109.6
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP20896

DRAMP20896 chydropathy plot
    • Function

    • Antifungal activity.
  • ·Literature 1
    • Title

    • Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4.
    • Reference

    • PLoS One. 2017 Oct 17;12(10):e0186442.
    • Author

    • Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD.