• DRAMP ID

    • DRAMP20862
    • Peptide Name

    • rtCATH2(5-40)
    • Source

    • Synthetic construct
    • Family

    • Derived from Cathelicidins
    • Gene

    • Not found
    • Sequence

    • RRGKDSGGPKMGRKNSKGGWRGRPGSGRPGFGSGI
    • Sequence Length

    • 39
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic
    • Biological Activity

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

      • [Ref.27818338]Gram-negative bacteria:Escherichia coli (ATCC 25922)(MIC=16μM);A. salmonicida (ATCC 33658)(MIC=16μM);Y. ruckeri (NCIMB 1315)(MIC=16μM);
      • Gram-positive bacteria:Staphylococcus aureus (ATCC 25923)(MIC=64μM)
    • Hemolytic Activity

      • [Ref.27818338] No hemolytic activity to human
    • 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

    • Unconventional feature
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP20862 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP20862.
    • Formula

    • C150H249N59O43S
    • Absent Amino Acids

    • ACEHLQTVY
    • Common Amino Acids

    • G
    • Mass

    • 3599.06
    • PI

    • 12.31
    • Basic Residues

    • 10
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 3
    • Net Charge

    • +9
    • Boman Index

    • -11682
    • Hydrophobicity

    • -1.546
    • Aliphatic Index

    • 11.14
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 161.76
    • Polar Residues

    • 17

DRAMP20862

DRAMP20862 chydropathy plot
    • Function

    • Antibacterial activity against the Gram-positive and Gram-negative bacteria.The peptides inhibit the growth of V. anguillarum or A. hydrophila (MIC >32
  • ·Literature 1
    • Title

    • Antimicrobial and host cell-directed activities of Gly/Ser-rich peptides from salmonid cathelicidins.
    • Reference

    • Fish Shellfish Immunol. 2016 Dec;59:456-468.
    • Author

    • D'Este F, Benincasa M, Cannone G, Furlan M, Scarsini M, Volpatti D, Gennaro R, Tossi A, Skerlavaj B, Scocchi M.