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 - DFBPANOX0279(Antioxidative peptide)

DFBP ID	DFBPANOX0279
Peptide sequence	VLPVPQK
Type	Native peptide
Peptide/Function name	Antioxidative peptide, PEP^[3]

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	Antithrombotic activity ^[D1], DPP IV-inhibitory activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Val-Leu-Pro-Val-Pro-Gln-Lys

Single-letter amino acid

VLPVPQK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
780.5 Da	779.98 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.2286^c

Hydrophilic residue ratio

71.43%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protiens, Bovine
Precursor protein	β-Casein
Residue position	f(170-176)
Precursor protein(s) search	Source.1: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR8489 ---- Milk proteins ---- Beta-casein
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 petpide showed inhibition activity against Lox-catalyzed linoleate oxidation (initial rate kinetics) amounted to 10%.
Results indicated that daily administration of antioxidative peptide PEP at 50 and 100 μg/kg for 8 wk prevents body weight gain, uterine weight loss, and atrophy of endometrial lumen. Moreover, PEP increased femur dry weight, ash weight, bone ash calcium, and serum calcium and phosphorus level. Interestingly, PEP increased bone mineral density and improved trabecular microarchitecture in both femur and tibia of ovariectomized (OVX) rats. Additionally, PEP increased bone strength, reduced serum bone turnover markers, inhibited bone resorbing cytokines and decreased malondialdehyde level in OVX rat. Furthermore, PEP-elevated serum transforming growth factor-β, increased, reduced glutathione levels, superoxide dismutase, and catalase activity altered by OVX ^[3].

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])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Peptide obtained by hydrolysis of bovine b-casein (Eurial, Rennes, France) by use of trypsin.

Stability & Cytotoxicity

Peptide stability

Literature report:

Table 1. Difference in the availability of amino acid after digestion by proteases in-silico for VLPVPQK ^[4].
Serial No	Name of enzyme	No. of cleavages	Positions of cleavage
1	Lys C	1	7
2	Lys N	1	6
3	Pepsin (pH 1.3)	1	2
4	Pepsin (pH > 2)	1	2
5	Proteinase K	3	1,2,4
6	Trypsin	1	7
7	Caspase 1-10	-	-

EHP-Tool:

Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

Researchers demonstrated that PEP exhibits antiosteopenic effects via enhancement of antioxidant activity and reduction of bone-resorbing cytokines expression ^[3].

Database cross-references

DFBP

[D1]	DFBPANTH0161
[D2]	DFBPDPIV0189
[D3]	DFBPMUFU0658

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Rival SG, Fornaroli S, Boeriu CG, Wichers HJ. Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties. J Agric Food Chem. 2001 Jan;49(1):287-94. PMID: 11170590 DOI: 10.1021/jf000392t
Other literature(s)	[1] Ha, G.E., et al., Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563. Korean Journal for Food Science of Animal Resources, 2015. 35(6): p. 738-747. [2] Rival, S. G., S. Fornaroli, C. G. Boeriu, and H. J. Wichers. 2000. Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties. J. Agric. Food Chem. 48:27–32. [3] Mada S B , Reddi S , Kumar N , et al. Antioxidative peptide from milk exhibits anti-osteopenic effects through inhibition of oxidative damage and bone-resorbing cytokines in ovariectomized rats[J]. Nutrition, 2017, 43:21. [4] Devi, S., Pal, G.K., Kapila, R., Kapila, S. C-terminal sequence deletion effect on antioxidative characteristics of VLPVPQK bioactive peptide from buffalo milk casein. Lwt. 2020, 119.
PubDate	2001