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 - DFBPANHY0002(Antihypertensive peptide)

DFBP ID	DFBPANHY0002
Peptide sequence	LHLPLP
Type	Native peptide
Peptide/Function name	Antihypertensive peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Leu-His-Leu-Pro-Leu-Pro

Single-letter amino acid

LHLPLP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
688.4 Da	688.85 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.79 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.8333^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	β-Casein
Residue position	f(133-138)
Precursor protein(s) search	Source.1: DFBPPR3187 ---- Plant proteins ---- Probable glucuronosyltransferase Os10g0205300 Source.2: DFBPPR7605 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7665 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.5: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.6: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.7: DFBPPR8489 ---- Milk proteins ---- Beta-casein Source.8: DFBPPR16270 ---- Animal proteins ---- AP-4 complex subunit mu-1 Source.9: DFBPPR19085 ---- Animal proteins ---- AP-4 complex subunit mu-1
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

Antihypertensive activity

In vitro experiments	Dose (mg/kg)	SBP Decreases (Maximal)	DBP Decreases (Maximal)
SHR	2	21.87 ± 4.51 mmHg	28.5 ± 3.20 mmHg
Time	—	4 h	2 h

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Milk was fermented with Enterococcus faecalis, CECT 5727.

Stability & Cytotoxicity

Peptide stability

Literature report:	The peptide has the resistant to gastrointestinal digestion^[5].
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

The potential of the peptide for use in functional foods to mitigate hypertension would seem to merit further clinical studies in humans.

Database cross-references

DFBP

[D1]	DFBPACEI0420, DFBPACEI1478
[D2]	DFBPMUFU0117

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Quirós, A., Ramos, M., Muguerza, B., Delgado, M.A., Miguel, M., Aleixandre, A., et al. Identification of novel antihypertensive peptides in milk fermented with Enterococcus faecalis. International Dairy Journal. 2007, 17, 33-41. DOI: 10.1016/j.idairyj.2005.12.011
Other literature(s)	[1] Hernandezledesma B, Quiros A, Amigo L, et al. Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin[J]. International Dairy Journal, 2007, 17(1):42-49. [2] Kohmura M, Nio N, Kubo K, et al. Inhibition of angiotensin-converting enzyme by synthetic peptides of human. BETA.-casein[J]. Journal of the Agricultural Chemical Society of Japan, 1989, 53(8):2107-2114. [3] Miguel, M., et al., Changes in arterial blood pressure in hypertensive rats caused by long-term intake of milk fermented by Enterococcus faecalis CECT 5728. British Journal of Nutrition, 2005. 94(1): p. 36-43. [4] SánchezRivera, Laura, Ferreira Santos P , Miralles B , et al. Peptide fragments from β-casein f(134–138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity[J]. Food Research International, 2016, 88:348-353. [5] Quirós A, Del M C M , Ramos M , et al. Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.[J]. Peptides, 2009, 30(10):1848-1853. [6] Martinez-Maqueda, D., et al., Antihypertensive peptides from food proteins: a review. Food Funct, 2012. 3(4): p. 350-361.
PubDate	2007