• DRAMP ID

    • DRAMP01064
    • Peptide Name

    • Anticancerous peptide 1 (Cr-ACP1; Plants)
    • Source

    • Cycas revoluta (Sago palm)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • AWKLFDDGV
    • Sequence Length

    • 9
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.21882228]Gram-positive bacteria: Staphylococcus epidermidis (MIC=60 µM), Bacillus subtilis (MIC=30 µM);
      • Gram-negative bacteria: Pseudomonas aeruginosa (MIC=30 µM), EEscherichia coli strain ATCC 8739 (MIC=30 µM).
    • Hemolytic Activity

      • [Ref.21882228] Hemocompatibility study revealed the effectiveness of both the peptides where it showed no significant lysis of normal RBC cells compare to positive control (Triton X-100). Cr-ACP1 induced hemolysis of 7% at the conentration of 1 mM.
    • Cytotoxicity

      • [Ref.21882228] IC50 = 1.5 mM in Hep2 (Human epidermoid cancer cells); IC50 = 0.9 mM in HCT15 (human colon carcinoma cells HCT15); Cr-ACP1 induced a cell viability of 66% at the concentration of 4 mM.
    • Binding Target

    • DNA
    • 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

    • DRAMP01064 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01064.
    • Formula

    • C50H71N11O14
    • Absent Amino Acids

    • CEHIMNPQRSTY
    • Common Amino Acids

    • D
    • Mass

    • 1050.18
    • PI

    • 4.21
    • Basic Residues

    • 1
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 5
    • Net Charge

    • -1
    • Boman Index

    • -5.97
    • Hydrophobicity

    • 0.044
    • Aliphatic Index

    • 86.67
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 687.5
    • Polar Residues

    • 1

DRAMP01064

    • Function

    • The synthetic peptide inhibits cell proliferation and induces apoptosis in cancer-derived cell lines Hep2 (IC50=1.5 mM) and HCT15 and, to a lesser extent, in non-cancerous NIH/3T3 cells. The mode of action is presumably an arrest in the G0/G1 phase. Antiproliferative, proapoptotic and DNA-binding activities are increased by acetylation at Ala-1 and Lys-3. Has a weak hemolytic activity against mouse erythrocytes. Has antibacterial activity. Antibacterial activity is decreased by acetylation.
  • ·Literature 1
    • Title

    • Identification and characterization of a bactericidal and proapoptotic peptide from Cycas revoluta seeds with DNA binding properties.
    • Reference

    • J Cell Biochem. 2012 Jan;113(1):184-193.
    • Author

    • Mandal SM, Migliolo L, Das S, Mandal M, Franco OL, Hazra TK.