Photo-immobilization of a phospholipid polymer for surface modification
Photo-immobilization of a phospholipid polymer for surface modification
复制标题
DOI：
10.1016/j.biomaterials.2004.04.047
复制
发表时间：
2005-04-01
期刊：
影响因子：
14
通讯作者：
Ito, Y
中科院分区：
文献类型：
--
作者：
Konno, T;Hasuda, H;Ito, Y
制备了具有磷脂极性基团的光反应性聚合物，并将聚合物光固定在聚合物表面上，研究了其与生物组分的相互作用。通过使用光固定化方法，该聚合物用于聚乙烯和聚丙烯的表面改性，这些聚合物的表面在我们先前开发的磷酰胆碱衍生的聚合物中未被处理。以2-甲基丙烯酰氧乙基磷酰胆碱和甲基丙烯酸共聚物为原料，通过偶联反应合成了对叠氮基苯胺光反应性聚合物。当聚合物未图案化固定在表面上时，进行X射线光电子能谱分析和静态接触角测量。结果表明，表面覆盖着磷脂极性基团。使用微图案化光掩模进行微图案固定。使用原子力显微镜的测量表明，溶胀的微图案化聚合物的厚度是干燥聚合物的五倍。蛋白质吸附和血小板粘附减少的聚合物固定区域。哺乳动物细胞没有粘附，并在固定区域上形成聚集体。总之，光反应性磷脂聚合物共价固定在常规聚合物表面上，并且其倾向于减少与蛋白质和细胞的相互作用。(C)2004 Elsevier Ltd.保留所有权利。
A photo-reactive polymer having a phospholipid polar group was prepared, and the polymer was photo-immobilized on polymeric surfaces, where its interactions with biocomponents were investigated. By using a photo-immobilization method, the polymer was used for surface modification of polyethylene and polypropylene, polymers whose surfaces were not treated in our previous development of the phosphorylcholine-derived polymer. The photo-reactive polymer was synthesized by a coupling reaction involving copolymer consisting of 2-methacryloyloxyethyl phosphorylcholine and methacrylic acid with 4-azidoaniline. When the polymer was unpattern immobilized on the surface, X-ray photo-electron spectroscopic analysis and static contact angle measurements were performed. It was shown that the surface was covered with phospholipid polar groups. Micropattern immobilization was carried out using a micropatterned photo-mask. Measurements using atomic force microscopy showed that the swelled micropatterned polymer was five times as thick as the dried one. Protein adsorption and platelet adhesion were reduced on the polymer-immobilized regions. Mammalian cells did not adhere, and formed aggregates on the immobilized regions. In conclusion, the photo-reactive phospholipid polymer was covalently immobilized on the conventional polymer surfaces and it tended to reduce interactions with proteins and cells. (C) 2004 Elsevier Ltd. All rights reserved.