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 - DFBPHYCP0004(Hypocholesterolemic peptide)

DFBP ID	DFBPHYCP0004
Peptide sequence	VYVEELKPTPEGDLEILLQK
Type	Native peptide
Peptide/Function name	Hypocholesterolemic peptide

Function-activity relationship

Main bioactivity	Hypocholesterolemic activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Val-Tyr-Val-Glu-Glu-Leu-Lys-Pro-Thr-Pro-Glu-Gly-Asp-Leu-Glu-Ile-Leu-Leu-Gln-Lys

Single-letter amino acid

VYVEELKPTPEGDLEILLQK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2313.65 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.05 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.3150^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	β-Lactoglobulin
Residue position	f(41-60)
Precursor protein(s) search	Source.1: DFBPPR7714 ---- Milk proteins ---- Beta-lactoglobulin Source.2: DFBPPR8499 ---- Milk proteins ---- Beta-lactoglobulin
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

Hypocholesterolemic activity

By screening using Caco-2 cells and animal studies, the serum and liver cholesterol levels were significantly lower in rats fed β-lactoglobuline tryptic hydrolysate (LTH) than in those fed casein tryptic hydrolysate (CTH). The peptide VYVEELKPTPEGDLEILLQK was purified from the Fraction 21 and 25, so this peptide was a potential hypocholesterolemic peptide (Synthetic peptide not determined).
The inhibition of micellar solubility of cholesterol which causes the suppression of cholesterol absorption by a direct interaction between cholesterol mixed micelles, and LTH in the jejunal epithelia is part of the mechanism underlying the hypocholesterolemic action of LTH.

Table 1. Effects of Oral Administration of Casein Tryptic Hydrolysate (CTH), β-Lactoglobulin Tryptic Hydrolysate (LTH), β-Sitosterol, or IIAEK on Body and Liver Weights, Food Intake, Serum HDL, and LDL + VLDL-cholesterol in Rats ¹
	Group
	CTH	LTH	β-sitosterol	IIAEK
Body weight gain (g/4 days)	10.4 ± 0.4 ^a	10.5 ± 0.7 ^a	9.5 ± 0.8 ^a	8.7 ± 0.4 ^a
Liver weight (g/100 g body weight)	5.22 ± 0.07 ^b	5.37 ± 0.05 ^{a, b}	5.17 ± 0.10 ^b	5.54 ± 0.11 ^a
Food intake (day 3, g/day)	8.5 ± 0.2 ^a	8.7 ± 0.2 ^a	8.3 ± 0.3 ^a	8.4 ± 0.3 ^a
Serum (mg/dl)
Total cholesterol (a)	529.3 ± 14.4 ^a	441.3 ± 12.0 ^b	435.4 ± 12.8 ^b	328.7 ± 11.3 ^c
HDL cholesterol (b)	42.6 ± 1.6 ^b	50.5 ± 2.4 ^a	52.1 ± 1.7 ^a	47.5 ± 0.8 ^{a, b}
LDL + VLDL-cholesterol ²	486.7 ± 26.7 ^a	390.8 ± 22.9 ^b	383.3 ± 24.2 ^b	281.2 ± 20.6 ^c
Atherogenic Index (b)/(a)	0.08 ± 0.01 ^c	0.11 ± 0.01 ^b	0.12 ± 0.01 ^b	0.15 ± 0.01 ^a
¹ The data are means ± SEM (n = 7). Within a row, means with different superscript letters are significantly different (P < 0.05) by Duncan’s multiple range test. ² Values were calculated as follows: LDL ± VLDL cholesterol = Total cholesterol — HDL cholesterol.

FIG 1. Effects of fractionated peptides derived from β-lactoglobulin on cholesterol absorption in Caco-2 cells in vitro.

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])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)NCC(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)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	β-Lactoglobulin was hydrolyzed by porcine trypsin (Novo Industry, Bagsvaerd, Denmark) at pH 8.0 and 37℃ for 3 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	Nagaoka S, Futamura Y, Miwa K, Awano T, Yamauchi K, Kanamaru Y, Tadashi K, Kuwata T. Identification of novel hypocholesterolemic peptides derived from bovine milk beta-lactoglobulin. Biochem Biophys Res Commun. 2001 Feb 16;281(1):11-7. PMID: 11178953 DOI: 10.1006/bbrc.2001.4298
Other literature(s)	N.D
PubDate	2001