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 - DFBPANOX0668(Antioxidative peptide)

DFBP ID	DFBPANOX0668
Peptide sequence	VVLYR
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antihypertensive activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Val-Val-Leu-Tyr-Arg

Single-letter amino acid

VVLYR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
648.81 Da	648.80 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.2800^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Coconut (cocos nucifera L.)
Precursor protein	Coconut cake globulin
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR3071 ---- Plant proteins ---- ABC transporter G family member 45 Source.2: DFBPPR4966 ---- Plant proteins ---- Glycinin G5 Source.3: DFBPPR20191 ---- Animal proteins ---- 5-oxoprolinase Source.4: DFBPPR10642 ---- Animal proteins ---- Protein disulfide-isomerase A3 Source.5: DFBPPR10880 ---- Animal proteins ---- Golgi apparatus protein 1 Source.6: DFBPPR11266 ---- Animal proteins ---- Protogenin
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

Antioxidative activity	The peptide VVLYR exhibited good superoxide radical scavenging activity with a concentration-dependent increase. VVLYR had remarkably protection effect on EA.hy926 cells against H₂O₂ induced damage and showed the highest ability at concentration of 1.0 mg/mL (P < 0.05).
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Coconut cake globulin hydrolysates with high ACE inhibitory activity (52.16%) were obtained by the sequential digestion of alcalase, flavourzyme, pepsin and trypsin assisted by high pressure pretreatment.

Stability & Cytotoxicity

Peptide stability

Literature report:	The peptide exhibited relatively good stability against gastrointestinal enzyme digestion (pepsin and pancreatin).
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

Coconut cake globulin could be effectively bioconverted to produce bioactive peptides, which could be used as a functional food ingredient to control ACE activity.

Database cross-references

DFBP

[D1]	DFBPACEI1349
[D2]	DFBPANHY0099
[D3]	DFBPMUFU0334

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Li, Y., Zheng, Y., Zhang, Y., Liu, L., Zhao, S. Purification, characterization, synthesis, in vivo and in vitro antihypertensive activity of bioactive peptides derived from coconut (Cocos nucifera L.) cake globulin hydrolysates. RSC Advances. 2016, 6, 92688-98. DOI: 10.1039/c6ra19971b
Other literature(s)	N.D
PubDate	2016