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 - DFBPOPIO0106(Opioid peptide)

DFBP ID	DFBPOPIO0106
Peptide sequence	YPFPGP
Type	Native peptide
Peptide/Function name	Opioid peptide, β-Casomorphin-6

Function-activity relationship

Main bioactivity	Opioid activity
Otheir bioactivity	DPP IV-inhibitory activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Pro-Phe-Pro-Gly-Pro

Single-letter amino acid

YPFPGP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	676.76 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.6167^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protien
Precursor protein	β-Casein
Residue position	f(60-65)
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: 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

Opioid activity

The heptapeptide YPFPGP showed potently opioid agonist activity for μ-opiate receptor ^[1,3].

Table 1. Opioid activity of synthesis products, and, for comparison, peptides isolated from bovine casein peptone.
Substance	Opioid activity ^a
Substance	Synthesis product with free carbosyl group	Isolated product from casein peptone
YPFPGPI	57.0 ± 7.5	55.0 ± 6.9
YPFPGP	27.4 ± 1.7	－
YPFPG	6.5 ± 0.6	5.0 ± 0.8
YPFP	21.9 ± 2.6	－
YPF	> 200	> 200
YP	> 200	－
Methionine-enkephalin	0.19 ± 0.02	－
Normorphine	0.23 ± 0.02	－
^a The values indicate the substance concentrations in μΜ which effected a 50% inhibition of electrically induced contractions of the guinea pig ileum longitudinal muscle-myenteric plexus preparation. All inhibitons proved to be antagonisable by the specific opiate antagonist naloxone. For comparison methionine-enkephalin and normorphine are listed.

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)N1[C@@]([H])(CCC1)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Bovine milk protein was hydrolysis with pepsin.

Stability & Cytotoxicity

Peptide stability

Literature report:	The opioid peptide was highly resistant towards proteolysis, even by pronase.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

The sequence of bovine β-casein (59-81) is -LVYPFPGPI-Pro⁶⁷/His⁶⁷-NSLPQNIPPLTQTP- ^[5].

Database cross-references

DFBP

[D1]	DFBPDPIV0197
[D2]	DFBPMUFU0734

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Lottspeich F, Henschen A, Brantl V, Teschemacher H. Novel opioid peptides derived from casein (beta-casomorphins). III. Synthetic peptides corresponding to components from bovine casein peptone. Hoppe Seylers Z Physiol Chem. 1980 Dec;361(12):1835-9. PMID: 7461609 DOI: 10.1515/bchm2.1980.361.2.1835
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] Meisel H, Frister H, Schlimme E. Biologically active peptides in milk proteins.[J]. Zeitschrift Für Ernährungswissenschaft, 1989, 28(4):267. [3] Schlimme E, Meisel H. Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects.[J]. Nahrung, 1995, 39(1):1-20. [4] Jinsmaa Y., Yoshikawa M., Enzymatic release of neocasomorphin and β-casomorphin from bovine β-casein. Peptides, 1999, 20, 957–962. [5] Jinsmaa Y, Yoshikawa M. Enzymatic release of neocasomorphin and beta-casomorphin from bovine beta-casein.[J]. Peptides, 1999, 20(8):957.
PubDate	1980