Adsorption of plasma proteins to nanomaterial surfaces has a great influence on their bio-functionality. However, there is limited understanding of the relationship between the functional proteins in the protein coron...Adsorption of plasma proteins to nanomaterial surfaces has a great influence on their bio-functionality. However, there is limited understanding of the relationship between the functional proteins in the protein corona and the biological identity of the materials. Here we show that the in situ generated thrombin in the protein corona of a Ca-zeolite surface displays a calcium-dependent, unusually high （-3,000 NIH U/mg） procoagulant activity, which is even stable against antithrombin deactivation. Removing the encapsulated Ca^2＋ in the zeolites leads to deactivation by antithrombin. Our observations suggest that the thrombin activity can be regulated by the inorganic surface and cations. Most importantly, our discovery indicates the link between the biomolecules in the protein corona and the procoagulant activity of the materials, providing a new molecular basis for the procoagulant mechanism for zeolite hemostatics.展开更多
基金We are grateful to X. D. Xi, T. Wu, H. Hu, and Z. Z. Kang for helpful discussions, and P. Liu for technical help with western blot analysis. This work was supported by the National Natural Science Foundation of China （Nos. 20873122, 21222307, and 21003106）, Fok Ying Tung Education Foundation （No. 131015）, the Science ＆ Technology Department of Zhejiang Province （Nos. 2008C11125 and R12B030002）, and the Fundamental Research Funds for the Central Universities （No. 2014XZZX003-02）.
文摘Adsorption of plasma proteins to nanomaterial surfaces has a great influence on their bio-functionality. However, there is limited understanding of the relationship between the functional proteins in the protein corona and the biological identity of the materials. Here we show that the in situ generated thrombin in the protein corona of a Ca-zeolite surface displays a calcium-dependent, unusually high （-3,000 NIH U/mg） procoagulant activity, which is even stable against antithrombin deactivation. Removing the encapsulated Ca^2＋ in the zeolites leads to deactivation by antithrombin. Our observations suggest that the thrombin activity can be regulated by the inorganic surface and cations. Most importantly, our discovery indicates the link between the biomolecules in the protein corona and the procoagulant activity of the materials, providing a new molecular basis for the procoagulant mechanism for zeolite hemostatics.
