• DRAMP ID

    • DRAMP01081
    • Peptide Name

    • Alyteserin-1a (toads, amphibians, animals)
    • Source

    • Alytes obstetricans (European midwife toad)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • GLKDIFKAGLGSLVKGIAAHVAN
    • Sequence Length

    • 23
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

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

      • [Ref.19463738]Gram-negative bacterium: Escherichia coli (MIC=25 µM).
    • Hemolytic Activity

      • [Ref:19463738] LC50 > 100 μM against human erthrocytes. Alyteserin-1a induced a hemolysis of 11% at the concentration of 100 μM.
    • Cytotoxicity

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

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • α-Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L (to be determined)
    • Structure

    • Not found
    • Structure Description

    • Not found
    • PDB ID

    • None
    • DRAMP01081 helical wheel diagram
    • Formula

    • C104H175N29O28
    • Absent Amino Acids

    • CEMPQRTWY
    • Common Amino Acids

    • AG
    • Mass

    • 2279.71
    • PI

    • 9.7
    • Basic Residues

    • 4
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 12
    • Net Charge

    • +3
    • Boman Index

    • 6.59
    • Hydrophobicity

    • 0.63
    • Aliphatic Index

    • 127.39
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 6

DRAMP01081

DRAMP01081 chydropathy plot
    • Function

    • The alyteserin-1 peptides show selective growth inhibitory activity against the Gram-negative bacterium Escherichia coli. The hemolytic activity against human erythrocytes of all peptides tested is relatively weak.
    • Structural similarity

    • The alyteserin-1 peptides show limited structural similarity to the ascaphins from the skins of frogs of the family Leiopelmatidae.
  • ·Literature 1
    • Title

    • The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae).
    • Reference

    • Peptides. 2009 Jun;30(6):1069-1073.
    • Author

    • Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC.