General Information

    • DRAMP ID

    • DRAMP35966

    • Peptide Name

    • P2

    • Source

    • Synthetic

    • Family

    • Gene

    • Not found

    • Sequence

    • KRGDKA

    • Sequence Length

    • 6

    • Protein Existence

    • Not found

Activity Information

    • Biological Activity

    • Antimicrobial, Anticancer

    • Target Organism

      • Tumor cells: HepG2 (IC50=10.92µg/mL); HEp-2 (IC50=11.38µg/mL); MCF-7 (IC50=38.53µg/mL); A375 (IC50=91.28µg/mL)

    • Hemolytic Activity

      • Not available

    • Cytotoxicity

      • Vero: IC50=65.03µg/mL

    • Binding Target

    • Not available

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • α-(2,5,7-tri-tert-butyl) tryptophan (W*)

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP35966 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP35966.

Physicochemical Information

    • Formula

    • C27H51N11O9

    • Absent Amino Acids

    • CEFHILMNPQSTVWY

    • Common Amino Acids

    • K

    • Mass

    • 76314

    • PI

    • 10.79

    • Basic Residues

    • 3

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 1

    • Net Charge

    • +2

    • Boman Index

    • -3199

    • Hydrophobicity

    • -2.4

    • Aliphatic Index

    • 16.67

    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 1

DRAMP35966

Comments Information

    • The perceived cancer cell-selective killing of both peptides P1 and P2 seems to stalk from cationic peptides and the electrostatic interactions between the anionic lipids of cancer cells on account of specific binding between integrins proteins and N (APN/CD13) ligand-receptor on the cancer cell membrane and the presence of binding RGD and NGR motifs in peptides.

Literature Information

  • ·Literature 1

    • Title

    • Design and synthesis of novel N-terminal peptides of integrin and aminopeptidase are new finding for anticancer activity

    • Reference

    • Bioorg Chem. 2023 May;134:106435.

    • Author

    • Krishnamoorthy R, Singh M, Anaikutti P, Paul L E, Dhanasekaran S, Sathiah T.