Abstract：
:A novel food-derived anticoagulant heptapeptides (P-3-CG) was isolated and characterized from oyster (Crassostrea gigas) pepsin hydrolysate. P-3-CG competed with fibrinogen against thrombin active domain by a spontaneous and exothermic reaction which was entropically driven. The residue Lys7 of P-3-CG anchored thrombin S1 pocket strongly, which inhibited fibrinogen binding to the thrombin, then blocked the conversion of fibrinogen to fibrin. The fibrinogen clotting time was prolonged to 27.55 s, and the reciprocally authenticated results of dynamic light scattering and scanning electron microscope further explained for fibrinogen clotting time extension. Inhibition of amidolytic activity of thrombin was affected significantly by reaction time and P-3-CG concentration. Furthermore, P-3-CG prolonged activated partial thromboplastin time significantly in vitro/vivo, and decreased the mortality which was confirmed by pulmonary pathological slide results. The obtained results demonstrated that P-3-CG may potentially serve as an alternative food-derived anticoagulant peptide that could be utilized for thrombosis prevention.
journal_name
Food Chemjournal_title
Food chemistryauthors
Cheng S,Tu M,Liu H,An Y,Du M,Zhu Bdoi
10.1016/j.foodchem.2020.127507subject
Has Abstractpub_date
2021-01-01 00:00:00pages
127507eissn
0308-8146issn
1873-7072pii
S0308-8146(20)31369-8journal_volume
334pub_type
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