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List of peptide properties
DFBP ID - DFBPANTH0062(Antithrombotic peptide)
DFBP ID DFBPANTH0062
Peptide sequence PHPHLSF
Type Native peptide
Peptide/Function name Antithrombotic peptide
Function-activity relationship
Main bioactivity Antithrombotic activity
Otheir bioactivity Other bioactive activity [D1], Multifunctional activity [D2]
Calculated physicochemical properties
Three-letter amino acid Pro-His-Pro-His-Leu-Ser-Phe
Single-letter amino acid PHPHLSF
Peptide length 7
Peptide mass
Experimental mass Theoretical mass
N.D 833.94 Da c
Net charge 0.00 c
Isoelectric point (pI) 7.95 c
IC50 N.D
pIC50 N.D
GRAVY -0.5429 c
Hydrophilic residue ratio 57.14% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Cow milk protein
Precursor protein κ-Casein
Residue position

f(99-105)

Precursor protein(s) search
Link-research
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 was inhibitor of the chymosin digestion of cow κ-casein. As shown in table 1.

Table 1 Inhibition of the chymosin digestion of cow κ-casein in the presence of various synthetic peptides derived from κ-casein [2]
Sources
Peptide
Inhibition (%) of the amount of cow κ-caseinoglycopeptide liberated when cow κ-casein was digested by chymosin in the presence of synthetic peptides
3 mg peptide
4 mg peptide
Without

0
0
From cow κ-caseinPHPHLSF
30
+
Ac-PHLSF
31
44
PHLSF
47
94
Ac-HLSF
45
+
HLSF
16
32
Ac-LSF
41
38
MAIPPK
0
0
NQDK
0
0
MAIPPKKNQDK
0
0
LSFMAIPPK
< 10

From fibrinogen γ-chain
GPRP
0
0

+: Determination not possible as the peptide was not soluble in this concentration.
Ac: Acetyl.

Specific target protein(s) Specific Target Protein(s):
Chymosin
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Bitter taste prediction
SMILES N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O
Preparation method
Mode of preparation

Enzymatic hydrolysis

Enzyme(s)/starter culture

Hydrolysis with trypsin.

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
Additional information N.D
Database cross-references
DFBP
[D1] DFBPINPE0001
[D2] DFBPMUFU0721
BIOPEP-UWM [D3] 3203
APD [D4] -
BioPepDB [D5] -
MBPDB [D6] -
Reference(s)
Primary literature Fiat AM, Levy-Toledano S, Caen JP, Jollès P. Biologically active peptides of casein and lactotransferrin implicated in platelet function. J Dairy Res. 1989;56(3):351-5.
PMID: 2760301
Other literature(s)

[1] Xu, Ruo‐Jun. Bioactive Peptides in Milk and their Biological and Health Implications[J]. Food Reviews International, 1998, 14(1):1-16.
[2] 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.

PubDate 1989
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214