Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

DFBP ID - DFBPRENI0009(Renin-inhibitory peptide)

DFBP ID	DFBPRENI0009
Peptide sequence	PNECQL
Type	Native peptide
Peptide/Function name	Renin-inhibitory peptide

Function-activity relationship

Main bioactivity	Renin-inhibitory activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antihypertensive activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Pro-Asn-Glu-Cys-Gln-Leu

Single-letter amino acid

PNECQL

Peptide length

Peptide mass

Experimental mass	Theoretical mass
702 Da	702.78 Da ^c

Net charge

-1

Isoelectric point (pI)

3.30

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.9667^c

Hydrophilic residue ratio

33.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Rapeseed
Precursor protein	Cruciferin
Residue position	f(4-9)
Precursor protein(s) search	Source.1: DFBPPR7416 ---- Plant proteins ---- Cruciferin CRU4 Source.2: DFBPPR7417 ---- Plant proteins ---- Cruciferin Source.3: DFBPPR7444 ---- Plant proteins ---- Cruciferin BnC2 Source.4: DFBPPR7446 ---- Plant proteins ---- Cruciferin BnC1
Link-research Inductive analysis	There are no literature reports on the discovery of this sequence in other food-source proteins.

Biological/Functional activity & target protein

Renin-inhibitory activity	The final rapeseed protein hydrolysate (FRPH) exhibited potent Renin (EC:3.4.23.15) inhibitory activity with an IC₅₀ value of 0.47 ± 0.05 mg/mL. The peptide PNECQL was isolated from the FRPH using electrodialysis with ultrafiltration membrane (EDUF) technology, so it was a potential renin-inhibitory peptide (data not shown).
Specific target protein(s)	Specific Target Protein(s): Renin

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Rapeseed protein isolate was subjected to alcalase digestion to obtain a protein hydrolysate.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

DFBP

[D1]	DFBPACEI1413
[D2]	DFBPANHY0035
[D3]	DFBPMUFU0366

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	He R, Girgih AT, Rozoy E, Bazinet L, Ju XR, Aluko RE. Selective separation and concentration of antihypertensive peptides from rapeseed protein hydrolysate by electrodialysis with ultrafiltration membranes. Food Chem. 2016 Apr 15;197(Pt A):1008-14. PMID: 26617047 DOI: 10.1016/j.foodchem.2015.11.081
Other literature(s)	[1] He R , Alashi A , Malomo S A , et al. Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates[J]. Food Chemistry, 2013, 141(1):153-159.
PubDate	2016