Peptide name : Cecropin XJ

Source/Organism : Larvae of Bombyx mori

Linear/Cyclic : Linear

Chirality : L

Peptide length: 41

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information:

Assay type : MTT assay

Assay time : 24-h

Activity : Cell viability = 50% at 50 µmol/l

Cell line : Huh-7

Cancer type : Liver Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 4474.3243 Dalton

Aliphatic index : 0.929

Instability index : 68.6098

Hydrophobicity (GRAVY) : -0.339

Isoelectric point : 10.377

Charge (pH 7) : 5.7984

Aromaticity : 4.878

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

Hydrophobic/hydrophilic ratio : 1.5625

hydrophobic moment : 0.8566

Missing amino acid : C,H,Q,T,Y

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (41., 26., 26.)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)N)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)CC)C(C)C)[C@@H](C)CC)C(C)C

1 : Xia L, et al. The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells. Oncol Lett. 2016; 12:57-62. doi: 10.3892/ol.2016.4601

Paper title : The antibacterial peptide from Bombyx mori cecropinXJ induced growth arrest and apoptosis in human hepatocellular carcinoma cells.

Doi : https://doi.org/10.3892/ol.2016.4601

Abstract : CecropinXJ is a cationic antimicrobial peptide originally isolated from the larvae of Bombyx mori. The anticancer effect of cecropinXJ has been reported in various tumor cells, including leukemia, gastric and esophageal cancer cells. However, the activity of cecropinXJ on hepatocellular carcinoma (HCC) and its underlying mechanism have not been investigated to date. Therefore, the present study investigated the efficacy and associated mechanism of cecropinXJ in Huh-7 cells. Flow cytometric analysis was performed to determine the presence of cell cycle arrested and apoptotic cells. CecropinXJ significantly inhibited the growth of Huh-7 cells in a dose- and time-dependent manner. CecropinXJ treatment for 24 h induced S cell cycle arrest and apoptosis, in addition to loss of the mitochondrial membrane potential, in hepatoma cells. CecropinXJ induced HCC cell apoptosis by activating caspase-3 and poly(ADP-ribose) polymerase. Furthermore, cecropinXJ downregulated the expression of B-cell lymphoma 2 (Bcl-2), while upregulated the expression of Bcl-2-associated death promoter and Bcl-2-associated X protein. In conclusion, the results of the present study suggest that cecropinXJ may be an active anti-HCC agent and provide novel insights into the mechanism of cecropinXJ.