Current protein & peptide science · 2026
Preparation, Identification, and Anticoagulant and Antithrombotic Activities of Peptide-Rich Fractions from Crassostrea hongkongensis Hydrolysates.
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Zhu Qilin, Chen Suhua, Yang Fei
Аннотация
OBJECTIVE: Oysters are abundant in protein and represent a promising raw material for producing bioactive peptides. This work aimed to isolate antithrombotic peptide-rich fractions from Crassostrea hongkongensis meat and evaluate their anticoagulant and antithrombotic effects via in vitro clotting assays and mouse in vivo experiments.
METHODS: Enzymatic hydrolysis was performed to prepare EC. Sequential ultrafiltration and dialysis were adopted to obtain graded fractions FEC1-FEC5. In vitro clotting time assays were conducted to screen active fractions. FEC5 was further purified by Sephadex G-15 gel filtration to yield four subfractions (F1-F4) with different molecular weight distributions. Chemical composition, molecular spectral features, and molecular weight distribution of EC, FEC5, and F2 were characterized using UV scanning, FTIR spectroscopy, and UHPLC-QTOF-MS. A carrageenan-induced mouse tail thrombosis model was established to evaluate the in vivo antithrombotic potency of FEC5, indicated by IR and PCTE.
RESULTS: Among all subfractions, F2 possessed the highest peptide content (90.17%) and prolonged in vitro clotting time to 401.92 s, with anticoagulant activity approaching that of HSPCG (p > 0.05). The high-dose FEC5 group exhibited in vivo antithrombotic activity, with an IR of 41.98% and a PCTE of 43.63%. These indicators were numerically higher than those of the APDG without statistical significance (p > 0.05). UHPLC-QTOF-MS analysis confirmed eight shared peptide components between FEC5 and F2 with defined molecular weights. Characteristic marker ions of FEC5 remained detectable after gel filtration, yet residual system impurities existed in F2, indicating that single-round Sephadex G-15 purification cannot completely remove small-molecule contaminants. Chromatography also altered component distribution and molecular aggregation states. Typical peptide absorption signals and phenylalanine characteristic UV absorption were observed in EC, FEC5, and F2, and FTIR spectra displayed characteristic amide A and amide I bands.
DISCUSSION: The peptide-rich fractions from Crassostrea hongkongensis, especially FEC5, show obvious anticoagulant and antithrombotic effects in vitro and in vivo. FEC5 exhibited dosedependent activity, with its efficacy numerically close to aspirin, and high concentrations of FEC5 achieved anticoagulant activity comparable to heparin sodium in vitro. Further exploration is required to reveal its underlying action mechanisms.
CONCLUSION: FEC5 exerted dose-dependent anticoagulant and antithrombotic effects in vitro and in vivo. Further purification effectively improved the activity of its subfraction F2. The peptide-rich fractions from Crassostrea hongkongensis have potential for developing marine antithrombotic functional food ingredients.
METHODS: Enzymatic hydrolysis was performed to prepare EC. Sequential ultrafiltration and dialysis were adopted to obtain graded fractions FEC1-FEC5. In vitro clotting time assays were conducted to screen active fractions. FEC5 was further purified by Sephadex G-15 gel filtration to yield four subfractions (F1-F4) with different molecular weight distributions. Chemical composition, molecular spectral features, and molecular weight distribution of EC, FEC5, and F2 were characterized using UV scanning, FTIR spectroscopy, and UHPLC-QTOF-MS. A carrageenan-induced mouse tail thrombosis model was established to evaluate the in vivo antithrombotic potency of FEC5, indicated by IR and PCTE.
RESULTS: Among all subfractions, F2 possessed the highest peptide content (90.17%) and prolonged in vitro clotting time to 401.92 s, with anticoagulant activity approaching that of HSPCG (p > 0.05). The high-dose FEC5 group exhibited in vivo antithrombotic activity, with an IR of 41.98% and a PCTE of 43.63%. These indicators were numerically higher than those of the APDG without statistical significance (p > 0.05). UHPLC-QTOF-MS analysis confirmed eight shared peptide components between FEC5 and F2 with defined molecular weights. Characteristic marker ions of FEC5 remained detectable after gel filtration, yet residual system impurities existed in F2, indicating that single-round Sephadex G-15 purification cannot completely remove small-molecule contaminants. Chromatography also altered component distribution and molecular aggregation states. Typical peptide absorption signals and phenylalanine characteristic UV absorption were observed in EC, FEC5, and F2, and FTIR spectra displayed characteristic amide A and amide I bands.
DISCUSSION: The peptide-rich fractions from Crassostrea hongkongensis, especially FEC5, show obvious anticoagulant and antithrombotic effects in vitro and in vivo. FEC5 exhibited dosedependent activity, with its efficacy numerically close to aspirin, and high concentrations of FEC5 achieved anticoagulant activity comparable to heparin sodium in vitro. Further exploration is required to reveal its underlying action mechanisms.
CONCLUSION: FEC5 exerted dose-dependent anticoagulant and antithrombotic effects in vitro and in vivo. Further purification effectively improved the activity of its subfraction F2. The peptide-rich fractions from Crassostrea hongkongensis have potential for developing marine antithrombotic functional food ingredients.