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List of peptide properties
DFBP ID - DFBPANOX1141(Antioxidative peptide)
DFBP ID DFBPANOX1141
Peptide sequence YSNQNGRF
Type Native peptide
Peptide/Function name Antioxidative peptide
Function-activity relationship
Main bioactivity Antioxidative activity
Otheir bioactivity N.D
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
To calculate the physicochemical properties of bioactive peptide.
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
No matching precursor protein found
Link-research
There are no literature reports on the discovery of this sequence in other food-source proteins.
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
SMILES N.D
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.

Stability & Cytotoxicity
Peptide stability
Literature report: N.D
EHP-Tool: Enzymatic Hydrolysis Prediction Tool (EHP-Tool)
Peptide cytotoxicity
Literature report: N.D
Prediction: ToxinPred
Additional information
Additional information

These findings suggested that the antioxidant peptides from cottonseed protein had the potential as functional ingredients in foods.

Database cross-references
BIOPEP-UWM [D1] -
APD [D2] -
BioPepDB [D3] -
MBPDB [D4] -
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.
PMID: 33662918
Other literature(s) N.D
PubDate 2021
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214