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 - DFBPANHY0915(Antihypertensive peptide)

DFBP ID	DFBPANHY0915
Peptide sequence	PLIYP
Type	Native peptide
Peptide/Function name	Antihypertensive peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Pro-Leu-Ile-Tyr-Pro

Single-letter amino acid

PLIYP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	601.73 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.7600^c

Hydrophilic residue ratio

80%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Human
Organism/Source	Human milk protein
Precursor protein	β-Casein
Residue position	f(48-52)
Precursor protein(s) search	Source.1: DFBPPR1069 ---- Plant proteins ---- Cinnamoyl-CoA reductase 1 Source.2: DFBPPR5245 ---- Plant proteins ---- Omega-6 fatty acid desaturase, chloroplastic Source.3: DFBPPR7605 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR18347 ---- Animal proteins ---- Nucleolar complex protein 2 homolog Source.5: DFBPPR9220 ---- Animal proteins ---- Alpha-1D adrenergic receptor Source.6: DFBPPR12840 ---- Animal proteins ---- Alpha-1D adrenergic receptor
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

The peptide PLIYP was found to inhibit the pressor responses induced by angiotensin I, when administered i.v. to normotensive, urethanized rats.

Table 1. Inhibition of the pressor effects of Angiotensin I in vivo by the synthetic peptide fragments of human β-casein
Peptide^a	Dose (mg/kg, i.v.)	Max inhibition (%)
PLIYP	4	15
PLIYP	8	27
^a The single-letter notation for amino acids is used.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Synthesis
Enzyme(s)/starter culture	The peptides used in this study were synthesized by the conventional liquid-phase method.

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

DFBP

[D1]	DFBPACEI0385
[D2]	DFBPPEPI0055
[D3]	DFBPMUFU0409

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Kohmura, M., Nio, N., Kubo, K., Minoshima, Y., Munekata, E., Ariyoshi, Y. Inhibition of Angiotensin-converting Enzyme by Synthetic Peptides of Human β-Casein. Agricultural and Biological Chemistry. 2014, 53, 2107-14. DOI: 10.1080/00021369.1989.10869621
Other literature(s)	N.D
PubDate	2014