DFBP ID - DFBPANCA0320(Anticancer peptide) |
DFBP ID |
DFBPANCA0320 |
Peptide sequence |
LVPK |
Type |
Native peptide |
Peptide/Function name |
Anticancer peptide |
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Function-activity relationship |
Main bioactivity |
Anticancer activity |
Otheir bioactivity |
Antioxidative activity [D1], Multifunctional activity [D2] |
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Calculated physicochemical properties |
Three-letter amino acid |
Leu-Val-Pro-Lys |
Single-letter amino acid |
LVPK |
Peptide length |
4 |
Peptide mass |
Experimental mass |
Theoretical mass |
455.0 Da |
455.59 Da c |
|
Net charge |
0.00 c |
Isoelectric point (pI) |
10.04 c |
IC50 |
N.D |
pIC50 |
N.D |
GRAVY |
0.6250 c |
Hydrophilic residue ratio |
75% c |
Peptide calculator |
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Biological/Functional activity & target protein |
Anticancer activity |
The cancer cell antiproliferative activity of peptide fractions from black soybean protein was evaluated using MTT colorimetric assay. The final purified peptide fraction (F2-c) showed high cytotoxic potential against human liver (HepG2), lung (MCF-7) and cervical (Hela) cancer cells with the IC50
values of 0.22, 0.15 and 0.32 μM, respectively. The amino acid sequence
of F2-c was identified as Leu/Ile-Val-Pro-Lys (L/I-VPK).
Molecular docking studies revealed that the purified peptides effectively bound with four apoptosis related key proteins (XIAP, caspase-3, caspase-7, and Bcl-2) via hydrophobic effects and hydrogen bonds, amongst them, the peptide-caspase-3 binding showed the strongest binding energy.
The 3D structure of the BIR3 domain of XIAP (PDB code: 1g3f), the crystal structures of heterotetrameric active caspase-3 (PDB ID 1RHM) in complex with a nicotinic acid aldehyde inhibitor and unliganded caspase-7 (PDB ID 3IBF), the chain A of structure of Bcl-2 (PDB ID 2XA0) were derived from the RCSB PDB Protein Data Bank (http:// www.rcsb.org/pdb/home/home.do).
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Specific target protein(s) |
N.D |
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Taste properties & Structure |
Bitterness |
Literature report |
N.D |
Bitter prediction tools |
Bitter taste prediction |
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SMILES |
N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)O |
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Preparation method |
Mode of preparation |
Enzymatic hydrolysis
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Enzyme(s)/starter culture |
The protein hydrolysate was obtained by enzyme hydrolysis method with alcalase (EC 3.4.21.1, 20 × 104 U/g). |
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Stability & Cytotoxicity |
Peptide stability |
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Peptide cytotoxicity |
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Additional information |
Additional information |
The peptide fraction Leu/Ile-Val-Pro-Lys from black soybean byproduct with significant antioxidant and anticancer activities could be a good candidate for functional foods or related drugs. |
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Database cross-references |
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Reference(s) |
Primary literature |
Chen, Z., Li, W., Santhanam, R.K., Wang, C., Gao, X., Chen, Y., et al. Bioactive peptide with antioxidant and anticancer activities from black soybean [Glycine max (L.) Merr.] byproduct: isolation, identification and molecular docking study. European Food Research and Technology. 2018, 245, 677-89.
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Other literature(s) |
N.D |
PubDate |
2018 |
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