Peptide name : T Peptide

Source/Organism : Tuftsin derivative

Linear/Cyclic : Linear

Chirality : L

Peptide length: 19

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 48h

Activity : 67.2% maximum inhibitory rate at 8 mg/kg

Cell line : BGC-823

Cancer type : Gastric cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2332.8406 Dalton

Aliphatic index : 0

Instability index : -22.273

Hydrophobicity (GRAVY) : -2.868

Isoelectric point : 12

Charge (pH 7) : 10.3912

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 0.26666666

hydrophobic moment : -0.162

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

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : T

Least occurring amino acid frequency : 4

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.2, 0.2)

SMILES Notation: C[C@@H](O)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O

1 : An Y, et al. Anticancer activity of tuftsin-derived T peptide in postoperative residual tumors. Anticancer Drugs. 2014; 25:857-67. doi: 10.1097/CAD.0000000000000111

Paper title : Anticancer activity of tuftsin-derived T peptide in postoperative residual tumors.

Doi : https://doi.org/10.1097/CAD.0000000000000111

Abstract : Immune adjuvants have been used in cancer biotherapies to stimulate immune response to tumor cells. Despite their potential as anticancer reagents, there are several impediments to their use in clinical applications. In this study, we aim to modify the existing tuftsin structure and evaluate its antitumor activity in preclinical models. We synthesized a novel tuftsin derivative, namely, the T peptide (TP), by linking four tuftsin peptides, which showed enhanced stability in vivo. We then evaluated its anticancer activity in a postoperative residual tumor model in mice, where we surgically removed most of the primary tumor from the host, a procedure mimicking clinically postoperative patients. Despite the limited effect in intact solid tumors, TP strongly inhibited relapsed growth of residual tumors in postsurgical mice. Surgical resection of tumors accelerated residual tumor growth, but TP slowed down this process significantly. Interestingly, TP showed similar effects in human xenograft residual models. As an immunomodulator, TP could synergize the functions of macrophages, thus inhibiting the growth of cocultured tumor cells in vitro. Furthermore, TP could shift the macrophages to the tumor-suppressive M1 type and mobilize them to produce elevated cytotoxic TNF-α and NO. As a result, TP effectively prolonged the survival time of tumor-resected mice. Using the postoperative residual tumor models, we provide a body of evidence showing the antitumor activity of TP, which causes no obvious toxicity. Our study highlights the potential of TP as a postoperative adjuvant in cancer therapies.