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 - DFBPANTH0168(Antithrombotic peptide)

DFBP ID	DFBPANTH0168
Peptide sequence	FQSEEQQQTEDELQDK
Type	Native peptide
Peptide/Function name	Antithrombotic peptide

Function-activity relationship

Main bioactivity	Antithrombotic activity
Otheir bioactivity	Mineral-binding activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Phe-Gln-Ser-Glu-Glu-Gln-Gln-Gln-Thr-Glu-Asp-Glu-Leu-Gln-Asp-Lys

Single-letter amino acid

FQSEEQQQTEDELQDK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1982.00 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.49 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-2.3312^c

Hydrophilic residue ratio

12.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk (Bos taurus)
Precursor protein	α_s2-Casein
Residue position	f(9–27)
Precursor protein(s) search	Source.1: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR8489 ---- Milk proteins ---- Beta-casein
Link-research Inductive analysis	Link 1: DFBPANTH0130----Bovine milk (Bos taurus)----β-Casein

Biological/Functional activity & target protein

Antithrombotic activity	Molecular docking of peptide and thrombin (PDB: 2BVR): Affinity was observed for FQSEEQQQTEDELQDK with ‘‘-CDOCKER Energy” values of 252.387 kcal/mol, the peptide was a potential antithrombotic peptide (Antithrombotic activity of synthetic peptides was not determined).
Specific target protein(s)	Specific Target Protein(s): Prothrombin

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Design peptide
Enzyme(s)/starter culture	The peptide SSEESIISQETYKQEKNMA is designed based on the sequence TTI (fragment 36–39) and κ-casein (fragment 106– 116) ^[1].

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

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.

Database cross-references

DFBP

[D1]	DFBPMIBP0006
[D2]	DFBPMUFU0722

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Tu, M., Feng, L., Wang, Z., Qiao, M., Shahidi, F., Lu, W., et al. Sequence analysis and molecular docking of antithrombotic peptides from casein hydrolysate by trypsin digestion. Journal of Functional Foods. 2017, 32, 313-23. DOI: 10.1016/j.jff.2017.03.015
Other literature(s)	[1] Cappello, M., Bergum, P. W., Vlasuk, G. P., Furmidge, B. A., Pritchard, D. I., & Aksoy, S. (1996). Isolation and characterization of the tsetse thrombin inhibitor: A potent antithrombotic peptide from the saliva of Glossina morsitans morsitans. American Journal of Tropical Medicine and Hygiene, 54(5), 475–480.
PubDate	2017