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 - DFBPANTH0145(Antithrombotic peptide)

DFBP ID	DFBPANTH0145
Peptide sequence	SPAQILQWQVLSNTVPAK
Type	Native peptide
Peptide/Function name	Antithrombotic peptide

Function-activity relationship

Main bioactivity	Antithrombotic activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ser-Pro-Ala-Gln-Ile-Leu-Gln-Trp-Gln-Val-Leu-Ser-Asn-Thr-Val-Pro-Ala-Lys

Single-letter amino acid

SPAQILQWQVLSNTVPAK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1979.0840 Da	1980.28 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.0111^c

Hydrophilic residue ratio

55.56%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk (Bos taurus)
Precursor protein	κ-Casein
Residue position	f(69–86)
Precursor protein(s) search	Source.1: DFBPPR8492 ---- Milk proteins ---- Kappa-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	Molecular docking of peptide and thrombin (PDB: 2BVR): Affinity was observed for SPAQILQWQVLSNTVPAK with ‘‘-CDOCKER Energy” values of 161.249 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])(CO)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Thrombin inhibitory peptides from casein were screened by bioinformatics based on sequences predicted from in silico enzymatic digestion with trypsin, and identified by UPLC-Q-TOF-MS/MS with Mascot analysis.

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

[D1]

[D2]

[D3]

[D4]

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)	N.D
PubDate	2017