INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2026
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IF 8.7
Yanan Zhao,Kaiting Chen,Xiaofei He,Hui Guang,Kai Zong,Tianya Xue,Zhanfei She,Shuangqing Chen,Gaowa,Yongkuan Gong,Jinliang Gao
An anticoagulation coating was developed with tick-derived protein Qinghaienin. • The coating exhibits excellent hemocompatibility and anticoagulation activity. • Qinghaienin coating reduces non-specific protein or blood cells adsorption and inhibits FXII activation. Thrombus formation and thrombosis-related complications have consistently limited the safe use of blood-contacting medical devices in clinical practice. Qinghaienin, a novel tick-derived protein, inhibits activation of the intrinsic coagulation pathway by competing with factor XII for anionic surfaces. In this study, to create an anticoagulant coating, Qinghaienin was grafted onto the surface of commonly used medical polyvinyl chloride (PVC) material, which was premodified by polydopamine-polyethyleneimine (PDA-PEI). A series of studies verified that Qinghaienin immobilized on the PVC surface significantly enhanced the hydrophilicity of the material while retaining its biological activity. The PDA-PEI/Qinghaienin coating inhibited nonspecific protein adsorption, platelet adhesion, and thrombus formation in vitro . Furthermore, the PDA-PEI/Qinghaienin coating exhibited outstanding anticoagulant performance, which was superior to that of the PDA-PEI/Hep coating in static whole blood tests. In a rabbit arteriovenous shunt model, the coating effectively prolonged extracorporeal blood circulation time compared with control trials. These results demonstrate that the PDA-PEI/Qinghaienin coating exhibits excellent hemocompatibility and anticoagulant activity, highlighting its potential use in blood-contacting medical devices.
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DOI
PubMed
高影响因子
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
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2017
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IF 4.519
Junhui Li,Shan Li,Lufeng Yan,Tian Ding,Robert J. Linhardt,Yanlei Yu,Xinyue Liu,Donghong Liu,Xingqian Ye,Shiguo Chen
Fucosylated chondroitin sulfates (fCSs) are structurally unusual glycosaminoglycans isolated from sea cucumbers that exhibit potent anticoagulant activity . These fCSs were isolated from sea cucumber, Isostichopus badionotus and Pearsonothuria graeffei . Fenton reaction followed by gel filtration chromatography afforded fCS oligosaccharides , with different sulfation patterns identified by mass and NMR spectroscopy , and these were used to clarify the relationship between the structures and the anticoagulant activities of fCSs. In vitro activities were measured by activated partial thromboplastin time (APTT), thrombin time (TT), thrombin and factor Xa inhibition, and activation of FXII . The results showed that free radicals preferentially acted on GlcA residues affording oligosaccharides that were purified from both fCSs. The inhibition of thrombin and factor X activities, mediated through antithrombin III and heparin cofactor II of fCSs oligosaccharides were affected by their molecular weight and fucose branches. Oligosaccharides with different sulfation patterns of the fucose branching had a similar ability to inhibit the FXa by the intrinsic factor Xase (factor IXa-VIIIa complex). Oligosaccharides with 2,4- O -sulfo fucose branches from fCS- Ib showed higher activities than ones with 3,4- O -disulfo branches obtained from fCS- Pg . Furthermore, a heptasaccharide is the minimum size oligosaccharide required for anticoagulation and FXII activation. This activity was absent for fCS oligosaccharides smaller than nonasaccharides . Molecular size and fucose branch sulfation are important for anticoagulant activity and reduction of size can reverse the activation of FXII caused by native fCSs.
研究领域:
生物化学
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药理学
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DOI
高影响因子
Advanced Healthcare Materials
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2023
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IF 10
Chunyu Liu,Xu Cui,Yunbo Du,Xue Wang,Jua Kim,Shuaijie Li,Liyan Zhang,Xiaoli Zhao,Limin Zhao,Pengfei Tian,Hao Zhang,Kun Su,Xian Li,Haobo Pan
Activation of coagulation cascades, especially FX and prothrombin, prevents blood loss and reduces mortality from hemorrhagic shock. Inorganic salts are efficient but cannot stop bleeding completely in hemorrhagic events, and rebleeding carries a significant mortality risk. The coagulation mechanism of biominerals has been oversimplified in the past two decades, limiting the creation of novel hemostats. Here, at the interface, the affinity of proteins, the protease activity, fibrinolysis, hydration shell, and dynamic microenvironment are monitored at the protein level. Proteomic analysis reveals that fibrinogen and antithrombin III's affinity for kaolin's interface causes a weak thrombus and rebleeding during hemostasis. Inspiringly, amorphous bioactive glass (BG) with a transient-dynamic ion microenvironment breaches the hydration layer barrier and selectively and slightly captures procoagulant components of kiniogen-1, plasma kallikrein, FXII, and FXI proteins on its interface, concurrently generating a continuous biocatalytic interface to rapidly activate both intrinsic and extrinsic coagulation pathways. Thus, prothrombin complexes are successfully hydrolyzed to thrombin without platelet membrane involvement, speeding production of high-strength clots. This study investigates how the interface of inorganic salts assists in coagulation cascades from a more comprehensive micro-perspective that may help elucidate the clinical application issues of kaolin-gauze and pave the way to new materials for managing hemorrhage.
研究领域:
血液学
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材料科学
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生物医学工程
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蛋白质组学
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DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）