Peptide name : Peptide 5

Source/Organism : Synthetic peptide of four designed analogs of vasoactive intestinal peptide, bombesin

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: Not available

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: Aib : 1-amino-isobutyric acid, O: Ornithine, Pen:penicillamine, CyLeu:cycloleucine or 1-aminocyclopentane-1-carboxylic acid and disulfide bond between Cys and Pen

Assay type : MTT/MTS assay

Assay time : 24h

Activity : 18.2 % inhibition of cell proliferation at 10 nM

Cell line : KB

Cancer type : Oral cancer

Other activity : Not found

Amino Acid Composition Bar Chart : Not available

Molecular mass : Not available

Aliphatic index : Not available

Instability index : Not available

Hydrophobicity (GRAVY) : Not available

Isoelectric point : Not available

Charge (pH 7) : Not available

Aromaticity : Not available

Molar extinction coefficient (cysteine, cystine): Not available

Hydrophobic/hydrophilic ratio : Not available

hydrophobic moment : Not available

Missing amino acid : Not available

Most occurring amino acid : Not available

Most occurring amino acid frequency : Not available

Least occurring amino acid : Not available

Least occurring amino acid frequency : Not available

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Molecular descriptors: Not available

ADMET properties: Not available

1 : Prasad S, et al. Delivering multiple anticancer peptides as a single prodrug using lysyl-lysine as a facile linker. J Pept Sci. 2007; 13:458-67. doi: 10.1002/psc.867

Paper title : Delivering multiple anticancer peptides as a single prodrug using lysyl-lysine as a facile linker.

Doi : https://doi.org/10.1002/psc.867

Abstract : A large 40-residue precursor peptide (propeptide 5) was synthesized by linking together four designed anticancer peptide analogs to the neuropeptides: vasoactive intestinal peptide, somatostatin, bombesin and substance P, using enzyme cleavable lysyl-lysine linkers. On incubation with the enzyme trypsin, propeptide 5 was cleaved in a sequence-specific manner at the lysyl-lysine residues in the linker to release the individual peptide fragments which were identified by LC-MS. Another precursor peptide (propeptide 5a), consisting of two of the peptide analogs linked through lysyl-lysine linker, was also preferentially cleaved at the Lys-Lys site on incubation with the enzyme trypsin. Propeptide 5 showed potent anticancer activity, both in vitro and in vivo, which was greater than that of the individual component peptides. The enhanced activity suggests that the propeptide is possibly cleaved in the biological system at the lysyl-lysine site to yield the individual peptide analogs, which together show a synergistic effect. On the basis of these experimental findings, it can be concluded that pairs of basic amino acids such as Lys-Lys can be used as facile linkers for delivering multiple biologically active peptides.