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 - DFBPACEI0814(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0814
Peptide sequence	GVHGV
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Gly-Val-His-Gly-Val

Single-letter amino acid

GVHGV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	467.54 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.79 ^c

IC₅₀

2.00 uM

pIC₅₀

-0.301

GRAVY

0.8800^c

Hydrophilic residue ratio

80%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Pig
Precursor protein	Porcine plasma protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1584 ---- Plant proteins ---- Sucrose-phosphatase 2 Source.2: DFBPPR3766 ---- Plant proteins ---- Probable sucrose-phosphatase 1 Source.3: DFBPPR5891 ---- Plant proteins ---- Sucrose-phosphatase 1 Source.4: DFBPPR12129 ---- Animal proteins ---- 39S ribosomal protein L15, mitochondrial
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 exhibited strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 2.00 uM.
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

NCC(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)NCC(=O)N[C@@]([H])(C(C)C)C(=O)O

Preparation method

Mode of preparation	Extraction
Enzyme(s)/starter culture	Angiotensin converting enzyme (ACE) inhibitory peptide was isolated from supernatant of trichloroacetic acid treated pig plasma using gel filtration chromatography and reverse phase high pressure liquid chromatography.

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	Park, E., Won, M., Lee, H.H., Song, K.B. Angiotensin converting enzyme inhibitory pentapeptide isolated from supernatant of pig plasma treated by trichloroacetic acid. Biotechnology Techniques. 1996, 10, 479-80.
Other literature(s)	[1] Murray, B.A. and R.J. FitzGerald, Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Curr Pharm Des, 2007. 13(8): p. 773-91.
PubDate	1996