Peptide name : EGFR-lytic

Source/Organism : Synthetic Peptide

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 32

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : ELISA

Assay time : 60min

Activity : IC50 : 0.12 µM

Cell line : MDA-MB-231

Cancer type : Breast cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 3755.6256 Dalton

Aliphatic index : 0.943

Instability index : -5.4625

Hydrophobicity (GRAVY) : -0.225

Isoelectric point : 10.243

Charge (pH 7) : 7.8363

Aromaticity : 0.125

Molar extinction coefficient (cysteine, cystine): (9970, 9970)

Hydrophobic/hydrophilic ratio : 1.07692307

hydrophobic moment : 0.3381

Missing amino acid : C,R,M,E,F,S,D,A

Most occurring amino acid : K

Most occurring amino acid frequency : 6

Least occurring amino acid : H

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](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)CNC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](N)Cc1ccc(O)cc1)[C@@H](C)O)C(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)O

1 : Ohara K, et al. Characterization of antilytic peptide antibody: application for the detection of lytic-based hybrid peptide in serum samples. J Pept Sci. 2011; 17:493-8. doi: 10.1002/psc.1349

Paper title : Characterization of antilytic peptide antibody: application for the detection of lytic-based hybrid peptide in serum samples.

Doi : https://doi.org/10.1002/psc.1349

Abstract : We previously reported that a novel targeted drug termed hybrid epidermal growth factor receptor (EGFR)-lytic peptide, made by chemical conjugation of targeted binding peptide and cell-killing, lytic-peptide components, has selective cytotoxic activity that allows it to discriminate between normal and cancer cells. In addition, in vivo analysis revealed that this hybrid peptide displays significant antitumor activity in a xenograft model of human breast and pancreatic cancer in mice. Here, we characterized antilytic peptide antibody, which was raised from rabbit serum using the antigen of lytic peptide conjugated with keyhole limpet hemocyanin. It was found that antilytic peptide antibody is specific to the lytic peptide as assessed by both ELISA and surface plasmon resonance analysis and can also bind to EGFR-lytic peptide. Epitope mapping analysis using Biacore showed that two successive lysine regions in the lytic-peptide sequence are significant for recognition by this antibody. In addition, it was shown that this antibody can detect lytic-based hybrid peptide in serum samples from mouse blood and also in cultured breast cancer MDA-MB-231 cell samples by immunocytochemical staining experiments. It was found that the maximum concentrations of this peptide in serum were reached within 15-30 min of i.v. administration of EGFR-lytic peptide to mice. These results indicate that this antibody will be a useful tool for the detection of lytic-based peptides to investigate their in vivo stability and pharmacokinetics.