Peptide name : Peptide K22D

Source/Organism : A12L/A20L

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 26

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 1h

Activity : IC50 : 1.39 ± 0.02 µMol/L

Cell line : HeLa

Cancer type : Cervical cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 3033.6936 Dalton

Aliphatic index : 1.05

Instability index : 3.2923

Hydrophobicity (GRAVY) : -0.061

Isoelectric point : 10.778

Charge (pH 7) : 6.8403

Aromaticity : 0.115

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 0.78571428

hydrophobic moment : 0.1539

Missing amino acid : C,R,Q,P,M,E,D,Y,N,G

Most occurring amino acid : K

Most occurring amino acid frequency : 6

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)O

1 : Huang YB, et al. Role of helicity on the anticancer mechanism of action of cationic-helical peptides. Int J Mol Sci. 2012; 13:6849-6862. doi: 10.3390/ijms13066849

Paper title : Role of helicity on the anticancer mechanism of action of cationic-helical peptides.

Doi : https://doi.org/10.3390/ijms13066849

Abstract : In the present study, the 26-residue amphipathic α-helical peptide A12L/A20L (Ac-KWKSFLKTFKSLKKTVLHTLLKAISS-amide) with strong anticancer activity and specificity was used as the framework to study the effects of helicity of α-helical anticancer peptides on biological activities. Helicity was systematically modulated by introducing d-amino acids to replace the original l-amino acids on the non-polar face or the polar face of the helix. Peptide helicity was measured by circular dichroism spectroscopy and was demonstrated to correlate with peptide hydrophobicity and the number of d-amino acid substitutions. Biological studies showed that strong hemolytic activity of peptides generally correlated with high hydrophobicity and helicity. Lower helicity caused the decrease of anti-HeLa activity of peptides. By introducing d-amino acids to replace the original l-amino acids on the non-polar face or the polar face of the helix, we improved the therapeutic index of A12L/A20L against HeLa cells by 9-fold and 22-fold, respectively. These results show that the helicity of anticancer peptides plays a crucial role for biological activities. This specific rational approach of peptide design could be a powerful method to improve the specificity of anticancer peptides as promising therapeutics in clinical practices.