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 - DFBPANTH0103(Antithrombotic peptide)

DFBP ID	DFBPANTH0103
Peptide sequence	YQEPVLGPVRGPFPIIV
Type	Native peptide
Peptide/Function name	Antithrombotic peptide, Peptide 7

Function-activity relationship

Main bioactivity	Antithrombotic activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antihypertensive activity ^[D2], Antimicrobial activity ^[D3], Immunomodulatory activity ^[D4], Multifunctional activity ^[D5]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val

Single-letter amino acid

YQEPVLGPVRGPFPIIV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1880 Da	1881.24 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.88 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.4824^c

Hydrophilic residue ratio

76.47%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	β-Casein
Residue position	f(193-209)
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

Antithrombotic activity	The peptide showed a thrombin inhibition efficiency ratio of 4.6%/peptide concentration (μg/mL). Molecular docking of peptide and thrombin (PDB: 2BVR): Affinity was observed for YQEPVLGPVRGPFPIIV with ‘‘-CDOCKER Energy” values of 127.486 kcal/mol, the peptide was a potential antithrombotic peptide (Antithrombotic activity of synthetic peptides was not determined) ^[2].
Specific target protein(s)	Specific Target Protein(s): Prothrombin

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	The peptides was released from bovine caseins during fermentation by Lactobacillus casei Shirota.

Stability & Cytotoxicity

Peptide stability

Literature report:	Using ExPASy PeptideCutter tool and departing from peptide 7 sequence, it was determined that pepsin and trypsin would hydrolyse this peptide in fragments GPFPIIV and QEPVLGPVR.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

Sixty percent of the peptides identified in the casein hydrolysate showed good thrombin inhibitory activity. This method can be further developed to facilitate the rational production of bioactive peptides for their utilization in various functional food applications ^[2].

Database cross-references

DFBP

[D1]	DFBPACEI0427, DFBPACEI1401
[D2]	DFBPANHY0117
[D3]	DFBPAMIC0198
[D4]	DFBPIMMU0033
[D5]	DFBPMUFU0119

[D6]

[D7]

[D8]

[D9]

Reference(s)

Primary literature	Rojas-Ronquillo, R., Cruz-Guerrero, A., Flores-Nájera, A., Rodríguez-Serrano, G., Gómez-Ruiz, L., Reyes-Grajeda, J.P., et al. Antithrombotic and angiotensin-converting enzyme inhibitory properties of peptides released from bovine casein by Lactobacillus casei Shirota. International Dairy Journal. 2012, 26, 147-54. DOI: 10.1016/j.idairyj.2012.05.002
Other literature(s)	[1] Cheng, S., et al., Food-derived antithrombotic peptides: Preparation, identification, and interactions with thrombin. Crit Rev Food Sci Nutr, 2019: p. 1-15. [2] Tu M, Feng L, Wang Z, et al. Sequence analysis and molecular docking of antithrombotic peptides from casein hydrolysate by trypsin digestion[J]. Journal of Functional Foods, 2017, 32:313-323.
PubDate	2012