DFBP ID - DFBPANOX1141(Antioxidative peptide) |
DFBP ID |
DFBPANOX1141 |
Peptide sequence |
YSNQNGRF |
Type |
Native peptide |
Peptide/Function name |
Antioxidative peptide |
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Function-activity relationship |
Main bioactivity |
Antioxidative activity |
Otheir bioactivity |
N.D |
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Calculated physicochemical properties |
Three-letter amino acid |
Tyr-Ser-Asn-Gln-Asn-Gly-Arg-Phe |
Single-letter amino acid |
YSNQNGRF |
Peptide length |
8 |
Peptide mass |
Experimental mass |
Theoretical mass |
985.4254 Da |
985.02 Da c |
|
Net charge |
0.00 c |
Isoelectric point (pI) |
9.82 c |
IC50 |
N.D |
pIC50 |
N.D |
GRAVY |
-1.8375 c |
Hydrophilic residue ratio |
25% c |
Peptide calculator |
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Peptide source & Food-borne protein(s) search |
Classification |
Plant |
Organism/Source |
Cottonseed protein |
Precursor protein |
Vicilin GC72-A, Vicilin C72 |
Residue position |
f(399-406), f(395-402) |
Precursor protein(s) search
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No matching precursor protein found
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Link-research
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There are no literature reports on the discovery of this sequence in other food-source proteins. |
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Biological/Functional activity & target protein |
Antioxidative activity |
The cottonseed protein enzymatic hydrolysate with molecular weight less than 3 kDa exhibited excellent DPPH, ABTS and hydroxyl radical scavenging activity and ferrous ion chelating activity with EC50 values of 0.49 ± 0.02, 2.05 ± 0.02, 2.21 ± 0.12, and 0.99 ± 0.03 mg/mL, respectively. The peptide YSNQNGRF was extracted from this fraction and had the lowest CDOCKER energy and formed hydrogen bonds with Tyr334, Arg380, Arg415, Ser508, and Ser602, and van der Waals interactions with Asn382, Tyr525, Gln530, and Ser555, which all located in the binding site of Keap1-Nrf2 interaction. The X-ray crystal structure of human Keap1 (PDB code: 2FLU, resolution: 1.5 Å) was obtained from the RCSB Protein Data Bank and prepared and defined as the receptor. |
Specific target protein(s) |
N.D |
|
Taste properties & Structure |
Bitterness |
Literature report |
N.D |
Bitter prediction tools |
Non-bitter taste prediction |
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SMILES |
N.D |
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Preparation method |
Mode of preparation |
Enzymatic hydrolysis |
Enzyme(s)/starter culture |
Cottonseed protein was hydrolyzed by treating with Alcalase at enzyme/substrate ratio of 5000 U/g protein at 50 ◦C for 90 min under continuous mixing and subsequently boiled for 10 min to inactivate the protease. |
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Stability & Cytotoxicity |
Peptide stability |
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Peptide cytotoxicity |
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Additional information |
Additional information |
These findings suggested that the antioxidant peptides from cottonseed protein had the potential as functional ingredients in foods. |
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Database cross-references |
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Reference(s) |
Primary literature |
Wang L, Ma M, Yu Z, Du SK. Preparation and identification of antioxidant peptides from cottonseed proteins. Food Chem. 2021 Aug 1;352:129399.
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Other literature(s) |
N.D |
PubDate |
2021 |
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