通过原子力显微镜研究纤维蛋白原在金（111）表面自组装单分子层上的吸附。

Study of fibrinogen adsorption on self-assembled monolayers on Au(111) by atomic force microscopy.

作者信息

Lin Yi, Wang Jun, Wan Li-Jun, Fang Xiao-Hong

机构信息

Center of Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China.

出版信息

Ultramicroscopy. 2005 Nov;105(1-4):129-36. doi: 10.1016/j.ultramic.2005.06.028. Epub 2005 Jul 13.

DOI:10.1016/j.ultramic.2005.06.028

PMID:16095837

Abstract

The adsorption of plasma protein fibrinogen on the self-assembled monolayers (SAMs) of n-hexadecyl mercaptan and citrate was investigated with atomic force microscopy (AFM). On the basis of the preparation of these two flat SAMs on Au(111), high-resolution AFM images of bovine fibrinogen were obtained with different protein concentrations. The results indicated that the surface chemical composition significantly affected the adsorption behavior of fibrinogen. Since fibrinogen plays a key role in the regulation of both haemostasis and thrombosis, high-resolution AFM imaging on SAMs is expected to be an effective approach to study the haemocompatibility of materials with different surface chemistry.

摘要

利用原子力显微镜（AFM）研究了血浆蛋白纤维蛋白原在正十六烷基硫醇和柠檬酸盐自组装单分子层（SAMs）上的吸附情况。在金（111）表面制备这两种平整的自组装单分子层的基础上，获得了不同蛋白浓度下牛纤维蛋白原的高分辨率原子力显微镜图像。结果表明，表面化学成分显著影响纤维蛋白原的吸附行为。由于纤维蛋白原在止血和血栓形成的调节中起关键作用，因此在自组装单分子层上进行高分辨率原子力显微镜成像有望成为研究具有不同表面化学性质材料血液相容性的有效方法。