Department of Chemistry, Technical University of Denmark, DK-2800, Kongens Lyngby, Denmark.
Engineering Laboratory for Modern Analytical Techniques c/o State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, 130022, P. R. China.
Small. 2015 Nov 18;11(43):5814-25. doi: 10.1002/smll.201501819. Epub 2015 Sep 28.
Meeting proteins is regarded as the starting event for nanostructures to enter biological systems. Understanding their interactions is thus essential for a newly emerging field, nanomedicine. Chemically converted graphene (CCG) is a wonderful two-dimensional (2D) material for nanomedicine, but its stability in biological environments is limited. Systematic probing on the binding of proteins to CCG is currently lacking. Herein, we report a comprehensive study on the interactions between blood proteins and stabilized CCG (sCCG). CCG nanosheets are functionalized by monolayers of perylene leading to significant improvement in their resistance to electrolyte salts and long-term stability, but retain their core structural characteristics. Five types of model human blood proteins including human fibrinogen, γ-globulin, bovine serum albumin (BSA), insulin, and histone are tested. The main driving forces for blood protein binding involve the π-π interacations between the π-plane of sCCG and surface aromatic amonic acid (sAA) residues of proteins. Several key binding parameters including the binding amount, Hill coefficient, and binding constant are determined. Through a detailed analysis of key controlling factors, we conclude that the protein binding to sCCG is determined mainly by the protein size, the number, and the density of the sAA.
与蛋白质的结合被认为是纳米结构进入生物体系的起始事件。因此，了解它们的相互作用对于新兴的纳米医学领域至关重要。化学转化石墨烯（CCG）是纳米医学的一种理想的二维（2D）材料，但它在生物环境中的稳定性有限。目前缺乏对蛋白质与 CCG 结合的系统探测。在此，我们报告了关于血液蛋白与稳定化 CCG（sCCG）相互作用的综合研究。CCG 纳米片通过苝单层官能化，显著提高了其对电解质盐的抗性和长期稳定性，但保留了其核心结构特征。测试了五种类型的模型人血蛋白，包括人血纤维蛋白原、γ-球蛋白、牛血清白蛋白（BSA）、胰岛素和组蛋白。血液蛋白结合的主要驱动力涉及 sCCG 的π-平面与蛋白质表面芳香族碱性氨基酸（sAA）残基之间的π-π相互作用。确定了包括结合量、希尔系数和结合常数在内的几个关键结合参数。通过对关键控制因素的详细分析，我们得出结论，蛋白质与 sCCG 的结合主要取决于蛋白质的大小、sAA 的数量和密度。
