Peptide name : Chrysophsin-1

Source/Organism : The pyloric caeca and gills; Red sea bream

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 20

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTS assay, Lactate dehydrogenase (LDH) detection assay

Assay time : 24h

Activity : MIC : 7 µg/ml

Cell line : HT-1080

Cancer type : Human fibrosarcoma

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 2149.5805 Dalton

Aliphatic index : 1.32

Instability index : 12.015

Hydrophobicity (GRAVY) : 0.995

Isoelectric point : 10.002

Charge (pH 7) : 1.9325

Aromaticity : 0.15

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 4

hydrophobic moment : 0.6569

Missing amino acid : C,R,Q,T,P,M,E,S,D,Y,N,V

Most occurring amino acid : G

Most occurring amino acid frequency : 4

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.2, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)C(=O)O

1 : Hsu JC, et al. Characteristics of the antitumor activities in tumor cells and modulation of the inflammatory response in RAW264.7 cells of a novel antimicrobial peptide, chrysophsin-1, from the red sea bream (Chrysophrys major). Peptides. 2011; 32:900-10. doi: 10.1016/j.peptides.2011.02.013

Paper title : Characteristics of the antitumor activities in tumor cells and modulation of the inflammatory response in RAW264.7 cells of a novel antimicrobial peptide, chrysophsin-1, from the red sea bream (Chrysophrys major).

Doi : https://doi.org/10.1016/j.peptides.2011.02.013

Abstract : The antimicrobial peptide, chrysophsin-1, exhibits antimicrobial activities with similar efficiencies for both gram-negative and gram-positive bacteria. In this study, we examined the antitumor activity and modulation of the inflammatory response of a synthetic chrysophsin-1 peptide. In vitro results showed that chrysophsin-1 had greater inhibitory effects against human fibrosarcoma (HT-1080), histiocytic lymphoma (U937), and epithelial carcinoma (HeLa) cells. LDH release by HeLa cells was comparable to that of an MTS assay after treatment with 1.5-3 μg/ml chrysophsin-1 for 24h. Under SEM and TEM observations, we found no intact cell membranes after chrysophsin-1 treatment of HeLa cells for 8h. The suggested mechanism of the cytotoxic activity of chrysophsin-1 was disruption of cancer cell membranes. In addition, we also examined caspase-3, -8, and -9 activities by Western blotting; the results excluded the participation of apoptosis in chrysophsin-1's effect on HeLa cells. Stimulation by lipopolysaccharide induced tumor necrosis factor (TNF)-α which was able to modulate chrysophsin-1 treatment of RAW264.7 cells and inhibited endogenous TNF-α release but did not block its secretion. With data from this study, we demonstrate that chrysophsin-1 has antimicrobial and antitumor activities and modulates the inflammatory response in RAW264.7 cells.