General Information
-
DRAMP ID
- DRAMP35966
-
Peptide Name
- P2
-
Source
- Synthetic
-
Family
-
Gene
- Not found
-
Sequence
- KRGDKA
-
Sequence Length
- 6
-
UniProt Entry
- Notavailable
-
Protein Existence
- Not found
-
SMILES
- Not available
Activity Information
-
Biological Activity
- Antimicrobial, Anticancer
-
Target Organism
-
- Tumor cells:
Target Organism Activity HepG2 (IC50=10.92µg/mL); HEp-2 (IC50=11.38µg/mL); MCF-7 (IC50=38.53µg/mL); A375 IC50=91.28µg/mL
- Tumor cells:
-
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
-
Stereochemistry
- L
-
Structure
- Not found
-
Structure Description
- Not found
-
PDB ID
- Notavailable
-
Predicted Structure
- There is no predicted structure for DRAMP35966.
Physicochemical Information
-
Formula
Absent Amino Acids
Common Amino Acids
Mass
- 0
PI
- 0
Basic Residues
Acidic Residues
Hydrophobic Residues
Net Charge
-
Boman Index
- 0
Hydrophobicity
- 0
Aliphatic Index
- 0
Half Life
-
- Mammalian:
- Yeast:
- E.coli:
Extinction Coefficient Cystines
Absorbance 280nm
- 0
Polar Residues
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
-
Pubmed ID
- 36863075
-
Reference
- Bioorg Chem. 2023 May;134:106435.
-
Author
- Krishnamoorthy R, Singh M, Anaikutti P, Paul L E, Dhanasekaran S, Sathiah T.
