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 - DFBPANHY0013(Antihypertensive peptide)

DFBP ID	DFBPANHY0013
Peptide sequence	SLVSPSAAAAAAPGGS
Type	Native peptide
Peptide/Function name	Antihypertensive peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Ser-Leu-Val-Ser-Pro-Ser-Ala-Ala-Ala-Ala-Ala-Ala-Pro-Gly-Gly-Ser

Single-letter amino acid

SLVSPSAAAAAAPGGS

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1139.64 Da	1313.39 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.7250^c

Hydrophilic residue ratio

75%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Rapeseed
Precursor protein	Rapeseed protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR4007 ---- Plant proteins ---- Zinc-finger homeodomain protein 7
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

Antihypertensive activity	The effects of rapeseed peptides on blood pressure were measured in vivo in Goldblatt rat model of hypertension. The maximum difference in mean arterial pressure was approximately −50 mmHg in comparison to vehicle treated rats. The peptide was obtained from the hydrolyzsates, so the peptide may be a potential antihypertensive peptide.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CO)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)NCC(=O)N[C@@]([H])(CO)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Rapeseed meal proteins was hydrolyzed with Alcalase.

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

Rapeseed protein-derived peptides has the preventive potential against the progression of hypertension in vivo.

Database cross-references

DFBP

[D1]	DFBPACEI1319
[D2]	DFBPMUFU0322

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Mäkinen, S., Streng, T., Larsen, L.B., Laine, A., Pihlanto, A. Angiotensin I-converting enzyme inhibitory and antihypertensive properties of potato and rapeseed protein-derived peptides. Journal of Functional Foods. 2016, 25, 160-73. DOI: 10.1016/j.jff.2016.05.016
Other literature(s)	N.D
PubDate	2016