Identification and Antithrombotic Activity of Peptides from Blue Mussel (Mytilus edulis) Protein

Abstract

The blue mussel (Mytilus edulis) reportedly contains many bioactive components of nutritional value. Water-, salt- and acid-soluble M. edulis protein fractions were obtained and the proteins were trypsinized. The resultant peptides were analyzed by ultra-performance liquid chromatography quadrupole time of flight tandem mass spectrometry (UPLC-Q-TOF-MS/MS). 387 unique peptides were identified that matched 81 precursor proteins. Molecular mass distributions of the proteins and peptides were analyzed by sodium dodecyl sulfate-polyacryl amide gel electrophoresis (SDS-PAGE). The differences between the three protein samples were studied by Venn diagram of peptide and protein compositions. Toxicity, allergic and antithrombotic activity of peptides was predicted using database website and molecular docking respectively. The antithrombotic activity of enzymatic hydrolysate from water-, salt- and acid-soluble M. edulis protein were 40.17%, 85.74%, 82.00% at 5 mg/mL, respectively. Active mechanism of antithrombotic peptide (ELEDSLDSER) was also research about amino acid binding sites and interaction, simultaneously.

Evaluation of Anti-Inflammatory and Atheroprotective Properties of Wheat Gluten Protein Hydrolysates in Primary Human Monocytes

“…This result was only improved with Alcalase hydrolysis after 45 min (WGPH45A), which showed 25% thrombin-inhibitory activity. Although this value is not very high, similar results with Alcalase were reported in lupine protein hydrolysates [33], and in blue mussel proteins [39]. Taking together HD, ACE, and thrombin-inhibitory activity, we selected WGPH45A to analyze chemical and amino acidic composition and to evaluate biological activity in primary human monocytes.…”

Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development

“…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. As compared to enzymatic hydrolysis of proteins, there are only a few studies on fermentation of food proteins to obtain antithrombotic peptides and this provides a relatively interesting gap for researchers to explore.…”

Marine Bioactive Peptides—An Overview of Generation, Structure and Application with a Focus on Food Sources

“…For example, a high percentage of hydrophobic (aliphatic and aromatic) AA residues in antidiabetic peptides (Figure 4) [109][110][111] is necessary for inhibition of dipeptidyl peptidase IV, a key enzyme involved in degradation of incretins [110,112,113], and for recognition of receptors for glucagon-like peptides [114,115]. A high percentage of negatively charged AA residues (Figure 4) has been reported in antithrombotic peptides showing both direct thrombin inhibition [116,117] and inhibition of factors in intrinsic pathways [72,118]. A high frequency of positively charged AA residues in so-called cationic antimicrobial peptides ( Figure 4) [119][120][121] is proven to be necessary for interactions with anionic microbe membranes.…”