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 - DFBPOPIO0118(Opioid peptide)

DFBP ID	DFBPOPIO0118
Peptide sequence	YPFV
Type	Native peptide
Peptide/Function name	Opioid peptide, hβ-Casomorphin-4^[2]

Function-activity relationship

Main bioactivity	Opioid activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Tyr-Pro-Phe-Val

Single-letter amino acid

YPFV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	524.61 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.0250^c

Hydrophilic residue ratio

75%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Human
Organism/Source	Human milk protein
Precursor protein	β-Casein
Residue position	f(51-54)
Precursor protein(s) search	Source.1: DFBPPR1339 ---- Plant proteins ---- Glucosamine inositolphosphorylceramide transferase 1 Source.2: DFBPPR1592 ---- Plant proteins ---- Adenylosuccinate synthetase 1, chloroplastic Source.3: DFBPPR1599 ---- Plant proteins ---- Adenylosuccinate synthetase 2, chloroplastic Source.4: DFBPPR2974 ---- Plant proteins ---- Derlin-1 Source.5: DFBPPR3618 ---- Plant proteins ---- Putative auxin response factor 20 Source.6: DFBPPR4975 ---- Plant proteins ---- Beta-conglycinin beta subunit 1 Source.7: DFBPPR5014 ---- Plant proteins ---- Glycinol 4-dimethylallyltransferase Source.8: DFBPPR5035 ---- Plant proteins ---- Beta-conglycinin beta subunit 2 Source.9: DFBPPR5581 ---- Plant proteins ---- Adenylosuccinate synthetase, chloroplastic Source.10: DFBPPR6244 ---- Plant proteins ---- Carbonic anhydrase, chloroplastic Source.11: DFBPPR6675 ---- Plant proteins ---- Adenylosuccinate synthetase, chloroplastic Source.12: DFBPPR7196 ---- Plant proteins ---- Carbonic anhydrase, chloroplastic Source.13: DFBPPR7605 ---- Milk proteins ---- Beta-casein Source.14: DFBPPR16302 ---- Animal proteins ---- Myosin-2 Source.15: DFBPPR18255 ---- Animal proteins ---- Adenylosuccinate synthetase isozyme 2 Source.16: DFBPPR18876 ---- Animal proteins ---- Adenylosuccinate synthetase isozyme 1 Source.17: DFBPPR19190 ---- Animal proteins ---- Amiloride-sensitive sodium channel subunit gamma Source.18: DFBPPR19311 ---- Animal proteins ---- Dihydrodiol dehydrogenase 3 Source.19: DFBPPR19880 ---- Animal proteins ---- TATA box-binding protein-like 1 Source.20: DFBPPR20180 ---- Animal proteins ---- Peroxisome assembly protein 12 Source.21: DFBPPR21820 ---- Animal proteins ---- Mitochondrial carrier homolog 2 Source.22: DFBPPR21879 ---- Animal proteins ---- Protein SDA1 homolog Source.23: DFBPPR8870 ---- Animal proteins ---- Ribonuclease K3 Source.24: DFBPPR8942 ---- Animal proteins ---- Adenylosuccinate synthetase isozyme 2 Source.25: DFBPPR10065 ---- Animal proteins ---- Bifunctional purine biosynthesis protein ATIC Source.26: DFBPPR10429 ---- Animal proteins ---- Neuronal acetylcholine receptor subunit alpha-5 Source.27: DFBPPR10477 ---- Animal proteins ---- Aprataxin Source.28: DFBPPR10698 ---- Animal proteins ---- Adenylosuccinate synthetase isozyme 2 Source.29: DFBPPR11001 ---- Animal proteins ---- Neuronal acetylcholine receptor subunit beta-3 Source.30: DFBPPR11504 ---- Animal proteins ---- TATA box-binding protein-like 1 Source.31: DFBPPR13751 ---- Animal proteins ---- T-cell surface glycoprotein CD1b-2 Source.32: DFBPPR13816 ---- Animal proteins ---- T-cell surface glycoprotein CD1b-1 Source.33: DFBPPR13849 ---- Animal proteins ---- T-cell surface glycoprotein CD1b-3 Source.34: DFBPPR14092 ---- Marine protein ---- Adenylosuccinate synthetase isozyme 1 B Source.35: DFBPPR14094 ---- Marine protein ---- Adenylosuccinate synthetase isozyme 1 C Source.36: DFBPPR14101 ---- Marine protein ---- Adenylosuccinate synthetase isozyme 1 A Source.37: DFBPPR15138 ---- Microorganism protein ---- GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase Source.38: DFBPPR7767 ---- Plant protein ---- Adenylosuccinate synthetase 2, chloroplastic Source.39: DFBPPR7770 ---- Plant protein ---- Adenylosuccinate synthetase 1, chloroplastic
Link-research Inductive analysis	Link 1: DFBPOPIO0143----Soybean----β-Conglycinin β-Subunit Link 2: DFBPOPIO0148----Human milk protein----β-Casein

Biological/Functional activity & target protein

Opioid activity

YPFV was specific ligands for μ-opiate receptor and showed weak opioid agonist activity, the opioid activities was increased by the replacement of Val by _D-Val. YPFV-NH₂ and YPFV (_D-Val)-NH₂ showed more potent opioid activities. As shown in table 1.

Table 1 Opioid activity of peptides
Peptide	IC₅₀ (uM)			IC₅₀ MVD	Function
Peptide	RA^a	GPI^b	MVD^c	IC₅₀ GPI	Function
YPFV	170	19, 56.2^[5]	750	39.5	Opioid agonist
YPFV (_D-Val)	27	7.6	600	78.9
YPFV-NH₂	2.0	0.066	11.5	57.5
YPFV (_D-Val)-NH₂	0.58	0.060	28	165

^a Radioreceptor assay in the presence of 1 nM [³H]naloxone.
^b Guinea pig ileum assay.
^c Mouse vas deferens assay.

Specific target protein(s)

Specific Target Protein(s):
Mu-type opioid receptor

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C(C)C)C(=O)O

Preparation method

Mode of preparation	Synthesis peptide
Enzyme(s)/starter culture	Peptide was synthesized by a solid-phase method on chloromethyl resin.

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

(1) The peptide was also found in Soy β-Conglycinin β-Subunit ^[2].
(2) The human β-casomorphins are less potent than the bovine β-casomorphins in the GPI bioassay (i.e. their IC₅₀ values are higher) ^[5].

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Yoshikawa, M., Tani, F., Yoshimura, T., Chiba, H. Opioid Peptides from Milk Proteins. Agricultural and Biological Chemistry. 2014, 50, 2419-21. DOI: 10.1080/00021369.1986.10867763
Other literature(s)	[1] Kostyra E, Sienkiewiczszłapka E, Jarmołowska B, et al. Opioid peptides derived from milk proteins.[J]. Polish Journal of Food & Nutrition Sciences, 2004. [2] Kousaku OHINATA, Shun AGUI, Masaaki YOSHIKAWA. Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities[J]. Journal of the Agricultural Chemical Society of Japan, 2007, 71(10):2618-2621. [3] Chiba H, Yoshikawa M. Biologically functional peptides from food proteins: new opioid peptides from milk proteins[J]. Research, 1986. [4] Fiat A M, Jollès P. Caseins of various origins and biologically active casein peptides and oligosaccharides: Structural and physiological aspects[J]. Molecular & Cellular Biochemistry, 1989, 87(1):5-30. [5] Brantl, V., Novel opioid peptides derived from human beta-casein: human beta-casomorphins. European journal of pharmacology, 1984. 106(1): p. 213-214.
PubDate	2014