Lousinian S, Logothetidis S, Laskarakis A, Gioti M
Aristotle University of Thessaloniki, Department of Physics, GR-54124 Thessaloniki, Greece.
Biomol Eng. 2007 Feb;24(1):107-12. doi: 10.1016/j.bioeng.2006.05.014. Epub 2006 Jun 3.
Haemocompatibility is one of the most important properties, together with the tissue compatibility and corrosion and wear resistance that determine the biocompatibility of the artificial implants. Carbon-based thin films, such as amorphous carbon (a-C) and amorphous hydrogenated diamond-like carbon (a-C:H or DLC) are considered as excellent candidates for use as biocompatible coatings on biomedical implants. The aim of this work is the comparative study of the haemocompatibility of the a-C:H thin films developed by magnetron sputtering under various deposition conditions, the development of a methodology in order to study the haemocompatibility of thin films, the optical properties of the adsorbed proteins (human serum albumin and fibrinogen) and their adsorption mechanisms. Haemocompatibility and the optical properties of a-C:H thin films and the adsorbed proteins were studied by spectroscopic ellipsometry (SE). The films grown under floating conditions performed better haemocompatibility compared with those deposited under application of bias voltage. In the range of vis-UV, proteins are transparent, while they present an absorption peak at higher energies, but except these characteristics, their optical functions are rather featureless. Adsorption mechanisms were studied through AFM technique too. AFM results are in accordance with those derived by SE. Combination of the two techniques gives us a more accurate description of protein adsorption mechanisms.
血液相容性是最重要的特性之一,与组织相容性、耐腐蚀性和耐磨性共同决定了人工植入物的生物相容性。碳基薄膜,如非晶碳(a-C)和非晶氢化类金刚石碳(a-C:H或DLC),被认为是用于生物医学植入物生物相容性涂层的极佳候选材料。这项工作的目的是比较在各种沉积条件下通过磁控溅射制备的a-C:H薄膜的血液相容性,开发一种研究薄膜血液相容性的方法,研究吸附蛋白质(人血清白蛋白和纤维蛋白原)的光学性质及其吸附机制。通过光谱椭偏仪(SE)研究了a-C:H薄膜和吸附蛋白质的血液相容性及光学性质。与在施加偏压条件下沉积的薄膜相比,在浮动条件下生长的薄膜表现出更好的血液相容性。在紫外-可见光范围内,蛋白质是透明的,而在更高能量下它们会出现一个吸收峰,但除了这些特性外,它们的光学功能相当无特征。还通过原子力显微镜(AFM)技术研究了吸附机制。AFM结果与SE得出的结果一致。这两种技术的结合使我们能够更准确地描述蛋白质吸附机制。