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石英表面吸附的纤维蛋白原的分子与超分子结构以及纤维蛋白原的吸附等温线

Molecular and supramolecular structure of adsorbed fibrinogen and adsorption isotherms of fibrinogen at quartz surfaces.

作者信息

Nygren H, Stenberg M

机构信息

Department of Histology, University of Göteborg, Sweden.

出版信息

J Biomed Mater Res. 1988 Jan;22(1):1-11. doi: 10.1002/jbm.820220103.

Abstract

The adsorption of fibrinogen to quartz surfaces was measured by ellipsometry, ELISA, and electron microscopy. The initial adsorption at low concentrations was diffusion rate limited as determined by the ELISA and by counting the number of adsorbed molecules at electron micrographs. From ellipsometry, ELISA, and electron microscopy measurements it was found that the surface concentration of adsorbed fibrinogen increased continuously over four decades in bulk concentration of fibrinogen. At a hydrophilic quartz surface a plateau level of the adsorption isotherm was found at a surface concentration of 0.1 pmol/cm2 where the adsorbed molecules had a mean intermolecular distance of 10 +/- 5 nm between neighbors. At higher surface concentrations the molecules were densely packed and formed a layer where single molecules could not be identified. Adsorbed fibrinogen showed different structure at hydrophobic and hydrophilic quartz surfaces. At a hydrophilic surface, the fibrinogen molecules appeared as a 46 nm nodose rod consisting of 6-7 nodes with a diameter of 4 nm. At a hydrophobic surface, the molecule appeared as a binodular or trinodular rod with a node diameter of 5-9 nm, connected with a thin filament to form a 40-nm rod. Adsorption from higher concentrations of fibrinogen in solution resulted in adsorbed spheric structures with a diameter of 18-24 nm at the hydrophobic surface and in end-to-end polymers at the hydrophilic quartz membrane.

摘要

通过椭圆偏振法、酶联免疫吸附测定(ELISA)和电子显微镜测定了纤维蛋白原在石英表面的吸附情况。ELISA测定以及通过计算电子显微镜照片上吸附分子的数量确定,低浓度下的初始吸附受扩散速率限制。通过椭圆偏振法、ELISA和电子显微镜测量发现,在纤维蛋白原本体浓度的四个数量级范围内,吸附的纤维蛋白原的表面浓度持续增加。在亲水性石英表面,吸附等温线的平稳水平出现在表面浓度为0.1 pmol/cm²处,此时吸附分子的相邻分子间平均距离为10±5 nm。在较高表面浓度下,分子紧密堆积形成一层,无法识别单个分子。吸附在疏水性和亲水性石英表面的纤维蛋白原呈现出不同的结构。在亲水性表面,纤维蛋白原分子呈现为46 nm的结节状杆,由6 - 7个直径为4 nm的结节组成。在疏水性表面,分子呈现为双结节或三结节杆,结节直径为5 - 9 nm,通过细丝连接形成40 - nm的杆。从溶液中较高浓度的纤维蛋白原进行吸附,在疏水性表面产生直径为18 - 24 nm的吸附球形结构,在亲水性石英膜上产生端对端聚合物。

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