Peptide name : C3

Source/Organism : Synthetic construct

Linear/Cyclic : Linear

Chirality : L

Peptide length: Not available

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: (2,2-di(Nonephthalen-2-ylmethyl)-3-amino-propionic acid)

Assay type : MTT/MTS assay

Assay time : Not found

Activity : IC50 : 92 ± 2 µMol/L

Cell line : Ramos

Cancer type : Lymphoma 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 : Tørfoss V, et al. Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid. J Pept Sci. 2012; 18:609-19. doi: 10.1002/psc.2441

Paper title : Improved anticancer potency by head-to-tail cyclization of short cationic anticancer peptides containing a lipophilic β(2,2) -amino acid.

Doi : https://doi.org/10.1002/psc.2441

Abstract : We have recently reported a series of synthetic anticancer heptapeptides (H-KKWβ(2,2) WKK-NH(2) ) containing a central achiral and lipophilic β(2,2) -amino acid that display low toxicity against non-malignant cells and high proteolytic stability. In the present study, we have further investigated the effects of increasing the rigidity and amphipathicity of two of our lead heptapeptides by preparing a series of seven to five residue cyclic peptides containing the two most promising β(2,2) -amino acid derivatives as part of the central lipophilic core. The peptides were tested for anticancer activity against human Burkitt's lymphoma (Ramos cells), haemolytic activity against human red blood cells (RBC) and cytotoxicity against healthy human lung fibroblast cells (MRC-5). The results demonstrated a considerable increase in anticancer potency following head-to-tail peptide cyclization, especially for the shortest derivatives lacking a tryptophan residue. High-resolution NMR studies and molecular dynamics simulations together with an annexin-V-FITC and propidium iodide fluorescent assay showed that the peptides had a membrane disruptive mode of action and that the more potent peptides penetrated deeper into the lipid bilayer. The need for new anticancer drugs with novel modes of action is demanding, and development of short cyclic anticancer peptides with an overall rigidified and amphipathic structure is a promising approach to new anticancer agents.