Peptide name : LK2(5) (Temporin-1CEa Analog peptide)

Source/Organism : Synthetic construct

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 17

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT-assay

Assay time : 24h

Activity : IC50 : 44.7 µM

Cell line : MCF-7

Cancer type : Breast cancer

Other activity : Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 2020.4602 Dalton

Aliphatic index : 1.205

Instability index : 7.5882

Hydrophobicity (GRAVY) : -0.094

Isoelectric point : 10.176

Charge (pH 7) : 3.7562

Aromaticity : 0.117

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 0.88888888

hydrophobic moment : 0.0768

Missing amino acid : C,R,W,H,Q,T,P,M,E,Y,V,G

Most occurring amino acid : K

Most occurring amino acid frequency : 5

Least occurring amino acid : D

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.4)

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

1 : Yang QZ, et al. Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. Arch Pharm Res. 2013; 36:1302-10. doi: 10.1007/s12272-013-0112-8

Paper title : Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa.

Doi : https://doi.org/10.1007/s12272-013-0112-8

Abstract : Recent advances in the search for novel anticancer agents have indicated that the positively charged antimicrobial peptides have emerged as promising agents offering several advantages over the conventional anticancer drugs. As a naturally occurring, cationic, α-helical antimicrobial peptide, temproin-1CEa has been proved to exhibit a potent anticancer effect and a moderate hemolytic activity. In order to reduce the hemolytic activity of temporin-1CEa and improve its anticancer potency towards a range of human breast cancer cells, in the present study, six analogs of temporin-1CEa were rationally designed and synthesized. The amphipathicity levels and α-helical structural patterns of peptides were reserved, while their cationic property and hydrophobicity were changed. The results of MTT and hemolysis assay indicated that the analog peptides displayed an improved anticancer activity and showed an overall optimized therapeutic index. The hydrophobicity of peptides was positively correlated with their hemolytic and antitumor activities. Moreover, the data suggest a strategy of increasing the cationicity while maintaining the moderate hydrophobicity of naturally occurring amphipathic α-helical peptides to generate analogs with improved cytotoxicity against tumor cells but decreased activity against non-neoplastic cells such as human erythrocytes. This work highlights the potential for rational design and synthesis of improved antimicrobial peptides that have the capability to be used therapeutically for treatment of cancers.