Journal of the science of food and agriculture · 2025
A novel phosvitin anticoagulant peptide: preparation, identification and interaction with thrombin.
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Zhang Yaxin, Lv Binfei, Gao Shan, Ru Jingjing, Zhang Xiaowei
Аннотация
BACKGROUND: Searching for natural phosphorylated peptides as thrombin inhibitors is a good strategy for coagulation intervention. Phosvitin is one of the most phosphorylated proteins and has an anticoagulant effect by inhibiting thrombin.
RESULTS: The preparation of phosvitin hydrolysate was optimized by two-step enzymatic hydrolysis in this study, resulting in a significant enhancement of its thrombin inhibitory activity. After chromatography purification, the P4 fraction exhibiting the highest thrombin inhibitory activity was isolated. It significantly prolonged the thrombin time and the activated partial thromboplastin time, indicating inhibition of the endogenous and common coagulation pathways. pSSKpSSNpSpSK, identified from the P4 fraction, exhibited a high proportion among total peptides and strong thrombin affinity, primarily binding to exosite I of thrombin via electrostatic interactions. Polyphosphorylation of peptides played a critical role in thrombin inhibition. Additionally, pSSKpSSNpSpSK may interfere with blood coagulation through the lipid and atherosclerotic signaling pathway.
CONCLUSION: The present study successfully isolated polyphosphorylated peptides from phosvitin, demonstrating that their core components exert anticoagulant effects by inhibiting thrombin and interfering with signaling pathways, laying a promising theoretical foundation for developing anticoagulant functional foods. © 2025 Society of Chemical Industry.
RESULTS: The preparation of phosvitin hydrolysate was optimized by two-step enzymatic hydrolysis in this study, resulting in a significant enhancement of its thrombin inhibitory activity. After chromatography purification, the P4 fraction exhibiting the highest thrombin inhibitory activity was isolated. It significantly prolonged the thrombin time and the activated partial thromboplastin time, indicating inhibition of the endogenous and common coagulation pathways. pSSKpSSNpSpSK, identified from the P4 fraction, exhibited a high proportion among total peptides and strong thrombin affinity, primarily binding to exosite I of thrombin via electrostatic interactions. Polyphosphorylation of peptides played a critical role in thrombin inhibition. Additionally, pSSKpSSNpSpSK may interfere with blood coagulation through the lipid and atherosclerotic signaling pathway.
CONCLUSION: The present study successfully isolated polyphosphorylated peptides from phosvitin, demonstrating that their core components exert anticoagulant effects by inhibiting thrombin and interfering with signaling pathways, laying a promising theoretical foundation for developing anticoagulant functional foods. © 2025 Society of Chemical Industry.