Peptide name : p120RasGAP (317-326)

Source/Organism : Not found

Linear/Cyclic : Linear

Chirality : L

Peptide length: 10

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Luciferase assay

Assay time : Not found

Activity : Not found

Cell line : MCF-7

Cancer type : Human malignant mesothelomia

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1321.5032 Dalton

Aliphatic index : 0.68

Instability index : 19.93

Hydrophobicity (GRAVY) : -0.48

Isoelectric point : 6.0877

Charge (pH 7) : -0.2356

Aromaticity : 0.2

Molar extinction coefficient (cysteine, cystine): (11000, 11000)

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : 0.1111

Missing amino acid : C,H,Q,P,I,E,K,S,F,Y,A,G

Most occurring amino acid : W

Most occurring amino acid frequency : 2

Least occurring amino acid : M

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.2, 0.6)

SMILES Notation: CSCC[C@H](NC(=O)[C@@H](N)Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)[C@@H](C)O)[C@@H](C)O)C(C)C

1 : Michod D, et al. A RasGAP-derived cell permeable peptide potently enhances genotoxin-induced cytotoxicity in tumor cells. Oncogene. 2004; 23:8971-8. doi: 10.1038/sj.onc.1207999

Paper title : A RasGAP-derived cell permeable peptide potently enhances genotoxin-induced cytotoxicity in tumor cells.

Doi : https://doi.org/10.1038/sj.onc.1207999

Abstract : Treatment of many cancers relies on the combined action of several genotoxins, but the detrimental effect of these drugs on normal cells can cause severe side effects. One major challenge in anticancer therapy is therefore to increase the selectivity of current treatments toward cancer cells in order to spare normal cells. We have recently demonstrated that a RasGAP caspase cleavage fragment is able to sensitize HeLa cells towards cisplatin-induced apoptosis. Here, we extend this observation by showing that this fragment also enhances cell death induced by adriamycin and mitoxantrone, two other widely used genotoxins. Furthermore, we have delineated a short sequence within this fragment that still bears the genotoxin-sensitization property. The peptide encoded by this sequence, when fused to the TAT cell permeation sequence, potently sensitized a number of tumors cells, but not normal cells, towards apoptosis induced by cisplatin, adriamycin and mitoxantrone. This sensitization effect was not mediated through modulation of NFkappaB activity or activation of the JNK and p38 MAPK pathways. Our results demonstrate the feasibility in enhancing the efficacy of currently used drugs to selectively kill cancer cells using peptides derived from pro-apoptotic caspase substrate fragments.