dbacp06947
General Description
Peptide name : LJP-1
Source/Organism : Laminaria japonica
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : EGFHL
Peptide length: 5
C-terminal modification: Linear
N-terminal modification : Free
Non-natural peptide information:
Activity Information
Assay type : MTT assay
Assay time : 48-h
Activity : IC50 = 0.45 ± 0.05 mM
Cell line : HepG-2
Cancer type : Liver Cancer
Other activity : Anticancer
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 601.6513 Dalton
Aliphatic index : 0.78
Instability index : 8
Hydrophobicity (GRAVY) : -0.1
Isoelectric point : 5.2434
Charge (pH 7) : -1.076
Aromaticity : 20
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 1.5
hydrophobic moment : -0.950
Missing amino acid : A,C,D,I,K,M,N,P,Q,R,S,T,V,W,Y
Most occurring amino acid : E
Most occurring amino acid frequency : 1
Least occurring amino acid : E
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (40, 20, 40)
SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](Cc1ccccc1)NC(=O)CNC(=O)[C@@H](N)CCC(=O)O)C(=O)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | TTHHH |
| Chou-Fasman (CF) | CCCCC |
| Neural Network (NN) | CCCCH |
| Joint/Consensus | CCCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
CancerPPD : Not available
ApIAPDB : Not available
CancerPPD2 ID: 6906
Reference
1 : Wu Y, et al. Laminaria japonica Peptides Suppress Liver Cancer by Inducing Apoptosis: Possible Signaling Pathways and Mechanism. Mar Drugs. 2022; 20:(unknown pages). doi: 10.3390/md20110704
Literature
Paper title : Laminaria japonica Peptides Suppress Liver Cancer by Inducing Apoptosis: Possible Signaling Pathways and Mechanism.
Doi : https://doi.org/10.3390/md20110704
Abstract : The anticancer properties of Laminaria japonica peptides (LJPs) have never been studied. Here, we extracted LJPs from fresh seaweed and explored their anti-liver cancer activity (in vivo and in vitro). LJPs were isolated/purified by HPLC-ESI-MS. HepG2 cell apoptosis and cell cycle were evaluated. MTT assays were used to examine the cytotoxicity of LJPs. Caspase activation of caspases 3 and 9, cleaved caspases 3 and 9, and cleaved PARP was examined by Western blotting. The PI3K/AKT pathway and the phosphorylation states of MAPKs (p38 and JNK) were examined. We found that the LJP-1 peptide had the most antiproliferative activity in H22 cells in vitro. LJP-1 blocked H22 cells in the G0/G1 phase, accompanied by inhibition of cyclin expression. LJP-1 induced apoptosis through caspase activation and regulation of the ASK1/MAPK pathway. Concurrent in vivo studies demonstrated that LJP-1 significantly inhibited tumor growth and induced tumor cell apoptosis/necrosis. In conclusion, LJPs, particularly LJP-1, exert strong inhibitory effects on liver cancer growth in vivo and in vitro. LJP-1 induces HCC cell apoptosis through the caspase-dependent pathway and G0/G1 arrest. LJP-1 induces caspase-dependent apoptosis, in part by inhibiting PI3K, MAPK signaling pathways, and cell cycle proteins. LJP-1 has the potential to be a novel candidate for human liver cancer therapeutics.