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 - DFBPACEI1319(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1319
Peptide sequence	SLVSPSAAAAAAPGGS
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive 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

ACE-inhibitory activity	The peptide was a potential Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory peptide (data not shown).
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

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:	N.D
Prediction:	ToxinPred

Additional information

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

Database cross-references

DFBP

[D1]	DFBPANHY0013
[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