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 - DFBPANTH0007(Antithrombotic peptide)

DFBP ID	DFBPANTH0007
Peptide sequence	NQDK
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

Asn-Gln-Asp-Lys

Single-letter amino acid

NQDK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	503.51 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.71 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-3.6000^c

Hydrophilic residue ratio

0%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	κ-Casein
Residue position	f(113-116)
Precursor protein(s) search	Source.1: DFBPPR0839 ---- Plant proteins ---- Flavone 3'-O-methyltransferase 1 Source.2: DFBPPR1301 ---- Plant proteins ---- Proliferating cell nuclear antigen Source.3: DFBPPR1602 ---- Plant proteins ---- SNW/SKI-interacting protein A Source.4: DFBPPR1642 ---- Plant proteins ---- Ubiquitin-60S ribosomal protein L40-1 Source.5: DFBPPR1833 ---- Plant proteins ---- Ubiquitin-60S ribosomal protein L40-2 Source.6: DFBPPR3118 ---- Plant proteins ---- DNA polymerase delta small subunit Source.7: DFBPPR3425 ---- Plant proteins ---- Transcription initiation factor TFIID subunit 1 Source.8: DFBPPR3508 ---- Plant proteins ---- 60S ribosomal protein L5-1 Source.9: DFBPPR3642 ---- Plant proteins ---- Putative bidirectional sugar transporter SWEET7e Source.10: DFBPPR3839 ---- Plant proteins ---- Eukaryotic translation initiation factor isoform 4G-2 Source.11: DFBPPR4030 ---- Plant proteins ---- Cytochrome b5 Source.12: DFBPPR4109 ---- Plant proteins ---- 60S ribosomal protein L5-2 Source.13: DFBPPR5016 ---- Plant proteins ---- Protein SLE3 Source.14: DFBPPR5421 ---- Plant proteins ---- Pyruvate, phosphate dikinase regulatory protein, chloroplastic Source.15: DFBPPR5483 ---- Plant proteins ---- Caffeic acid 3-O-methyltransferase Source.16: DFBPPR6632 ---- Plant proteins ---- Tricetin 3',4',5'-O-trimethyltransferase Source.17: DFBPPR6644 ---- Plant proteins ---- Flavone O-methyltransferase 1 Source.18: DFBPPR7712 ---- Milk proteins ---- Lactoperoxidase Source.19: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.20: DFBPPR8206 ---- Plant proteins ---- DELLA protein GAIP-B Source.21: DFBPPR8492 ---- Milk proteins ---- Kappa-casein Source.22: DFBPPR8497 ---- Milk proteins ---- Lactoperoxidase Source.23: DFBPPR16040 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 Source.24: DFBPPR16123 ---- Animal proteins ---- Coiled-coil domain-containing protein 66 Source.25: DFBPPR17028 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 Source.26: DFBPPR17818 ---- Animal proteins ---- Endoribonuclease Dicer Source.27: DFBPPR17962 ---- Animal proteins ---- Ubiquitin carboxyl-terminal hydrolase isozyme L1 Source.28: DFBPPR20276 ---- Animal proteins ---- Hsp90 co-chaperone Cdc37-like 1 Source.29: DFBPPR20382 ---- Animal proteins ---- Ewing's tumor-associated antigen 1 homolog Source.30: DFBPPR21331 ---- Animal proteins ---- Proteasome maturation protein Source.31: DFBPPR22181 ---- Animal proteins ---- Tigger transposable element-derived protein 5 Source.32: DFBPPR22240 ---- Animal proteins ---- Ataxin-10 Source.33: DFBPPR8530 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 Source.34: DFBPPR8564 ---- Animal proteins ---- Ubiquitin carboxyl-terminal hydrolase isozyme L1 Source.35: DFBPPR9011 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 Source.36: DFBPPR9701 ---- Animal proteins ---- G-protein coupled receptor 39 Source.37: DFBPPR10199 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 Source.38: DFBPPR10289 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 Source.39: DFBPPR10559 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 Source.40: DFBPPR10705 ---- Animal proteins ---- Endoribonuclease Dicer Source.41: DFBPPR11042 ---- Animal proteins ---- Target of rapamycin complex 2 subunit MAPKAP1 Source.42: DFBPPR12276 ---- Animal proteins ---- Protein S100-A9 Source.43: DFBPPR12338 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 Source.44: DFBPPR12427 ---- Animal proteins ---- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 Source.45: DFBPPR12912 ---- Animal proteins ---- Junctophilin-1 Source.46: DFBPPR13261 ---- Animal proteins ---- Ubiquitin carboxyl-terminal hydrolase isozyme L1 Source.47: DFBPPR13676 ---- Animal proteins ---- Isocitrate dehydrogenase [NADP] cytoplasmic Source.48: DFBPPR14995 ---- Microorganism protein ---- ATP-dependent RNA helicase MSS116, mitochondrial Source.49: DFBPPR15132 ---- Microorganism protein ---- Amino-acid acetyltransferase, mitochondrial Source.50: DFBPPR15138 ---- Microorganism protein ---- GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
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

(1) The synthetic peptide NQDK inhibited the platelet aggregation but its effect was much lower than that induced by the undecapeptide (MAIPPKKNQDK). Around 400 μM of the NQDK were necessary to induce a 50% inhibition, i.e. four times more than for the MAIPPKKNQDK. At these concentrations the NQDK had no influence on fibrinogen binding. The effect of the natural peptide was similar (data not shown). So the NQDK is inhibitory but at higher doses (400 μM) than the MAIPPKKNQDK.
(2) The peptide is inhibitors of both, the aggregation of ADP-activated platelets and binding of human fibrinogen γ-chain to a specific receptor region on the platelet sufrace, but this peptide showed no inhibition for the chymosin digestion of cow κ-casein^[3].
(3) The interacting region of the fibrinogen γ-chain in platelet aggregation is the C-terminal dodecapeptide sequence that itself possesses similar inhibiting effects ^[4].
(4) The two smaller tryptic peptide MAIPPKK and NQDK contained in the undecapeptide (MAIPPKKNQDK) have a much lower effect on platelet aggregation and do not inhibit fibrinogen binding, as shown in Table 1 ^[6].

Table 1. Milk anti-aggregating peptides. Comparison with fibrinogen peptides.
Peptides	Inhibition (IC₅₀, μM)
Peptides	ADP-Induced human platelet aggregation	ADP-Induced [¹²⁵I]fibrinogen binding to human platelets
MAIPPKKNQDK	60	120
MAIPPKK	> 1600	﹣
NQDK	400	﹣

Specific target protein(s)

Specific Target Protein(s):
Fibrinogen gamma chain
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	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(CC(=O)N)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	Enzymatic hydrolysis
Enzyme(s)/starter culture	Chymosin digestion of cow κ-caein releases the κ-caseinoglycopeptide, the C-terminal part of κ-casein (residues 106-169). And then the κ-caseinoglycopeptide was digested 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	Jollès P, Lévy-Toledano S, Fiat AM, Soria C, Gillessen D, Thomaidis A, Dunn FW, Caen JP. Analogy between fibrinogen and casein. Effect of an undecapeptide isolated from kappa-casein on platelet function. Eur J Biochem. 1986 Jul 15;158(2):379-82. PMID: 3732274 DOI: 10.1111/j.1432-1033.1986.tb09764.x
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, 2010, 39(1):1-20. [3] Fiat A M, Levytoledano S, Caen J P, et al. Biologically active peptides of casein and lactotransferrin implicated in platelet function.[J]. Journal of Dairy Research, 1989, 56(3):351-355. [4] Kloczewiak M, Timmons S, Lukas T J, et al. Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain[J]. Biochemistry, 1984, 23(8):1767-74. [5] Meisel H. Overview on milk protein-derived peptides.[J]. International Dairy Journal, 1998, 8(5–6):363-373. [6] 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	1986