2019
DOI: 10.1080/10408398.2018.1524363
|View full text |Cite
|
Sign up to set email alerts
|

Food-derived antithrombotic peptides: Preparation, identification, and interactions with thrombin

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
28
0
3

Year Published

2019
2019
2023
2023

Publication Types

Select...
7
2
1

Relationship

0
10

Authors

Journals

citations
Cited by 47 publications
(38 citation statements)
references
References 146 publications
0
28
0
3
Order By: Relevance
“…These peptides are released by the action of proteolytic enzymes. Furthermore, it was observed that not only was the size of the peptide important for thrombin inhibition, but also the amino acid sequence, which might be homologous to the fibrinopeptides A and B from human fibrinogen (GGGVR-GP and PPSAR-GH, respectively) [26]. Therefore, antithrombotic activity is affected by the competition for platelet receptors between casoplatelin and the γ-chain of human fibrinogen (HHLGGAKQAGDV) [27,28], which is implicated in one of the three steps in thrombosis cascade reactions.…”
Section: Discussionmentioning
confidence: 99%
“…These peptides are released by the action of proteolytic enzymes. Furthermore, it was observed that not only was the size of the peptide important for thrombin inhibition, but also the amino acid sequence, which might be homologous to the fibrinopeptides A and B from human fibrinogen (GGGVR-GP and PPSAR-GH, respectively) [26]. Therefore, antithrombotic activity is affected by the competition for platelet receptors between casoplatelin and the γ-chain of human fibrinogen (HHLGGAKQAGDV) [27,28], which is implicated in one of the three steps in thrombosis cascade reactions.…”
Section: Discussionmentioning
confidence: 99%
“…It has been shown that antithrombotic peptides contain three to 20 amino acids residues and the peptides possess a certain homology of the γ‐chain of fibrinogen as they can compete for the receptors of the thrombocytes and subsequently inhibiting the formation or aggregation of platelets (Cheng et al., 2019; Zhang, 2016). To date, most of the food‐derived antithrombotic peptides are mainly obtained by either enzymatic hydrolysis or gastrointestinal digestion of milk casein (Liu et al., 2019; Tu et al., 2017), blue mussel (Qiao et al., 2018), legume (Chalé et al., 2016), amaranth grain (Sabbione et al., 2016), and brewer's spent grain (Cian et al., 2018) proteins.…”
Section: Structure–activity Relationship Of Bpsmentioning
confidence: 99%
“…Bioactive peptides from foods such as dairy products, seafood, seaweeds, nuts, cereals, and other natural sources possess antithrombotic properties that may be useful as antiplatelet agents as they seem to interact with multiple platelet activation pathways. These include inhibition of cyclooxygenase-1 (COX-1), inhibition of type-III collagen-induced aggregation, binding to glycoprotein IIb/IIIa, interacting with fibrinogen and its receptor, and affecting thrombin (73,74).…”
Section: Foods and Nutrients With Antithrombotic Propertiesmentioning
confidence: 99%