Peptide name : Peptide-20

Source/Organism : Synthetic Peptide

Linear/Cyclic : Cyclic(C1-C9)

Chirality : L

Peptide length: 9

C-terminal modification: Cyclic(C1-C9)

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 48h

Activity : At 100 µM 55% viablity

Cell line : MDA-MB-231

Cancer type : Breast cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1061.2199 Dalton

Aliphatic index : 0

Instability index : 115.333

Hydrophobicity (GRAVY) : -0.7

Isoelectric point : 8.0908

Charge (pH 7) : 0.9146

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 125)

Hydrophobic/hydrophilic ratio : 0.5

hydrophobic moment : -0.202

Missing amino acid : W,Q,P,I,E,K,F,D,Y,L,N,A,V,G

Most occurring amino acid : C

Most occurring amino acid frequency : 2

Least occurring amino acid : R

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.2, 0.1)

SMILES Notation: CSCC[C@H](NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CS)[C@@H](C)O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CS)C(=O)O

1 : Matsuo AL, et al. A novel melanoma-targeting peptide screened by phage display exhibits antitumor activity. J Mol Med (Berl). 2010; 88:1255-64. doi: 10.1007/s00109-010-0671-9

Paper title : A novel melanoma-targeting peptide screened by phage display exhibits antitumor activity.

Doi : https://doi.org/10.1007/s00109-010-0671-9

Abstract : Peptide display on the phage surface has been widely used to identify specific peptides targeting several in vivo and in vitro tumor cells and the tumor vasculature, playing a role in the discovery of bioactive antitumor agents. Bioactive peptides have been selected to target important tumor receptors or apoptosis-associated molecules such as p53. Presently, we attempted to identify potentially antitumor bioactive molecules using the whole cell surface as the recognizable static matrix. Such methodology could be advantageous in cancer therapy because it does not require previous characterization of target molecules. Using a C7C phage display library, we screened for peptides binding to the B16F10-Nex2 melanoma cell surface after pre-absorption on melan-A lineage. After a few rounds of enrichment, 50 phages were randomly selected, amplified, and tested for inhibition of tumor cell proliferation. Seven were active, and the corresponding peptide of each phage was chemically synthesized in the cyclic form and tested in vitro. Three peptides were able to preferentially inhibit the melanoma lineage. A unique peptide, [-CSSRTMHHC-], exhibited in vivo antitumor inhibitory activity against a subcutaneous melanoma challenge, rendering 60% of mice without tumor growth. Further, this peptide also markedly inhibited in vitro and in vivo the tumor cell invasion and cell-to-cell adhesiveness in vitro. This is the first report on a bioactive peptide derived from a C7C library active against whole melanoma cells in vitro and in vivo.