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 - DFBPACEI1793(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1793
Peptide sequence	VGGPR
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

Val-Gly-Gly-Pro-Arg

Single-letter amino acid

VGGPR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	484.56 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

11.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.5400^c

Hydrophilic residue ratio

80%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Marine bivalve
Organism/Source	Mactra veneriformis (Mactra veneriformis)
Precursor protein	M. veneriformis hydrolysates
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR3275 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 37 Source.2: DFBPPR3287 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 52B Source.3: DFBPPR4902 ---- Plant proteins ---- Endoribonuclease Dicer homolog 1 Source.4: DFBPPR5807 ---- Plant proteins ---- Histone H2A Source.5: DFBPPR20033 ---- Animal proteins ---- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 Source.6: DFBPPR10699 ---- Animal proteins ---- Acetylcholinesterase
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 VGGPR had essentially no effect on Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) activity (low activity, 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])(C(C)C)C(=O)NCC(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The M. veneriformis proteins were hydrolyzed by incubating with trypsin at pH 8.5 for 2 h at 40 ℃ at an enzyme to substrate ratio of 0.60% (w/w).

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	Liu R, Zhu Y, Chen J, Wu H, Shi L, Wang X, Wang L. Characterization of ACE inhibitory peptides from Mactra veneriformis hydrolysate by nano-liquid chromatography electrospray ionization mass spectrometry (Nano-LC-ESI-MS) and molecular docking. Mar Drugs. 2014 Jun 30;12(7):3917-28. PMID: 24983637 DOI: 10.3390/md12073917
Other literature(s)	N.D
PubDate	2014