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 - DFBPANTH0004(Antithrombotic peptide)

DFBP ID	DFBPANTH0004
Peptide sequence	LSFMAIPPK
Type	Native peptide
Peptide/Function name	Antithrombotic peptide, Casoplatelin

Function-activity relationship

Main bioactivity	Antithrombotic activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Leu-Ser-Phe-Met-Ala-Ile-Pro-Pro-Lys

Single-letter amino acid

LSFMAIPPK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1003.25 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.7667^c

Hydrophilic residue ratio

77.78%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	κ-Casein
Residue position	f(103-111)
Precursor protein(s) search	Source.1: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.2: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.3: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.4: 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

The peptide does inhibit platelet aggregation but not fibrinogen binding to ADP-treated platelets. Its also was a inhibitor of the chymosin digestion of cow κ-casein, but this peptide showed hardly any inhibition for the chymosin digestion of cow κ-casein, as shown in Table 1 ^[3].

Table 1 Inhibition of the chymosin digestion of cow κ-casein in the presence of various synthetic peptides derived from κ-casein
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
Sources	Peptide	3 mg peptide	4 mg peptide
Without	－	0	0
From cow κ-casein	PHPHLSF	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
Potential Target Protein(s):
Integrin beta-3
Integrin alpha-IIb
Integrin alpha-2
Platelet glycoprotein IX
Platelet glycoprotein Ib alpha chain
Platelet glycoprotein Ib beta chain
Platelet glycoprotein 4

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)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

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

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 DOI: 10.1017/S002202990002879X
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Schlimme E, Meisel H. Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects.[J]. Nahrung, 1995, 39(1):1-20. [3] 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. [4] Meisel H. Overview on milk protein-derived peptides.[J]. International Dairy Journal, 1998, 8(5–6):363-373. [5] Fiat A M, Migliore-Samour D, Jollã¨S P, et al. Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities[J]. Journal of Dairy Science, 1993, 76(1):301-310.
PubDate	1989