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 - DFBPACEI2234(ACE-inhibitory peptide)

DFBP ID	DFBPACEI2234
Peptide sequence	VIPVPFF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, V7

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Val-Ile-Pro-Val-Pro-Phe-Phe

Single-letter amino acid

VIPVPFF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	818.02 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

10.27 µM

pIC₅₀

-1.012

GRAVY

2.1857^c

Hydrophilic residue ratio

100%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Microorganism
Organism/Source	Yeast
Precursor protein	Yeast powder
Residue position	N.D
Precursor protein(s) search	No matching precursor protein found
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	(1) The peptide VIPVPFF exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity as a competitive inhibitor with an IC₅₀ value of 10.27 µM. (2) The peptide VIPVPFF increased the nitric oxide levels, upregulated GUCY1A1 gene expression (approximately 15-fold), and functioned in several hypertension-related pathways in human umbilical vein endothelial cells.
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N.D

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Yeast powder was mixed with crude enzyme (derived from B. subtilis) and distilled water at an enzyme/substrate ratio (E/S) of 7000 U/g. The hydrolysis was performed at 55 °C for 5 h.

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

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Huang Y, Jia F, Zhao J, Hou Y, Hu SQ. Novel ACE Inhibitory Peptides Derived from Yeast Hydrolysates: Screening, Inhibition Mechanisms and Effects on HUVECs. J Agric Food Chem. 2021 Mar 3;69(8):2412-2421. PMID: 33593053 DOI: 10.1021/acs.jafc.0c06053
Other literature(s)	N.D
PubDate	2021