Peptide name : Lytic

Source/Organism : Interleukin-4 receptor a (IL-4Ra) chain

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 17

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : WST-1 assay

Assay time : 24h

Activity : IC50 : 27.1 µMol/L

Cell line : H-322

Cancer type : Lung cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2061.8121 Dalton

Aliphatic index : 1.376

Instability index : -30.541

Hydrophobicity (GRAVY) : 0.1765

Isoelectric point : 10.845

Charge (pH 7) : 7.7521

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : -1.090

Missing amino acid : W,T,P,I,M,E,F,D,N,G,C,R,H,Q,S,Y,A,V

Most occurring amino acid : K

Most occurring amino acid frequency : 6

Least occurring amino acid : k

Least occurring amino acid frequency : 2

Secondary structure fraction (Helix, Turn, Sheet): (1, 0, 0.5)

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

1 : Yang L, et al. Targeting interleukin-4 receptor α with hybrid peptide for effective cancer therapy. Mol Cancer Ther. 2012; 11:235-43. doi: 10.1158/1535-7163.MCT-11-0363

Paper title : Targeting interleukin-4 receptor α with hybrid peptide for effective cancer therapy.

Doi : https://doi.org/10.1158/1535-7163.MCT-11-0363

Abstract : Interleukin-4 receptor α (IL-4Rα) chain is highly expressed on the surface of various human solid tumors. We designed a novel hybrid peptide termed IL-4Rα-lytic peptide that targets the IL-4Rα chain. The IL-4Rα-lytic peptide contains a target moiety to bind to IL-4Rα and a cellular toxic lytic peptide that selectively kills cancer cells. The anticancer activity of the IL-4Rα-lytic peptide was evaluated in vitro and in vivo. It was found that the IL-4Rα-lytic peptide has cytotoxic activity in cancer cell lines expressing IL-4Rα, determined by quantitative real-time PCR. The IC(50) ratios of the lytic peptide to the IL-4Rα-lytic peptide correlated well with the expression levels of IL-4Rα on cancer cells (r = 0.80). In addition, IL-4Rα-lytic peptide administered either intratumoraly or intravenously significantly inhibited tumor growth in xenograft model of human pancreatic cancer (BXPC-3) in mice. These results indicate that the IL-4Rα-lytic peptide generated in this study has a potent and selective anticancer potential against IL-4Rα-positive solid cancers.