General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.