• DRAMP ID

    • DRAMP01062
    • Peptide Name

    • Putative antimicrobial protein 3 (Cm-p2; Plants)
    • Source

    • Cenchritis muricatus (Beaded periwinkle)
    • Family

    • N/A
    • Gene

    • N/A
    • Sequence

    • SESILIVHQQQSRSSGS
    • Sequence Length

    • 17
    • Evidence code

    • Protein level
    • Biological Activity

    • Antifungal, Antimicrobial
    • Target Organism

      • No MICs found on DRAMP database
    • Hemolytic Activity

      • N/A
    • Cytotoxicity

    • Binding Target

    • N/A
    • Linear/Cyclic/Branched

    • N-terminal modification

    • C-terminal modification

    • Other modifications

    • Stereochemistry

    • Structure

    • N/A
    • Structure Description

    • N/A
    • DRAMP01062 helical wheel diagram
    • Formula

    • C75H127N25O29
    • Absent Amino Acids

    • ACDFKMNPTWY
    • Common Amino Acids

    • S
    • Mass

    • 2128.54
    • PI

    • 7.55
    • Basic Residues

    • 2
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 4
    • Boman Index

    • -43.67
    • Hydrophobicity

    • -58.24
    • Aliphatic Index

    • 85.88
    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 7

DRAMP01062

    • Function

    • This peptide demonstrated the capacity to prevent the development of yeasts and filamentous fungi. Otherwise, Cm-p1 displayed no toxic effects against mammalian cells.
  • Literature 1
    • Reference

    • Biochimie. 2012 Apr;94(4):968-974.
    • Author

    • L³pez-Abarrategui C, Alba A, Silva ON, Reyes-Acosta O, Vasconcelos IM, Oliveira JT, Migliolo L, Costa MP, Costa CR, Silva MR, Garay HE, Dias SC, Franco OL, Otero-Gonz¡lez AJ.
    • Title

    • Functional characterization of a synthetic hydrophilic antifungal peptide derived from the marine snail Cenchritis muricatus.