高等学校化学学报 ›› 2002, Vol. 23 ›› Issue (12): 2369.

• 研究论文 • 上一篇    下一篇

白蛋白原位复合的生物医用功能材料的研究(Ⅱ)──白蛋白的选择性吸附和血液相容性研究

计剑, 封麟先, 沈家骢   

  1. 浙江大学高分子科学与工程学系, 杭州310027
  • 收稿日期:2001-08-21 出版日期:2002-12-24 发布日期:2002-12-24
  • 通讯作者: 计 剑(1969年出生),男,博士,副教授,主要从事生物医用高分子、血液相容性材料、介入医用材料和组织工程材料的研究.E-mail:Jianji@mail.hz.z.jcn E-mail:Jianji@mail.hz.z.jcn
  • 基金资助:

    国家自然科学基金(批准号:298040)资助

In-situ Albumin Binding Material for Biomedical Application(Ⅱ)── Albumin Selectivity and in vitro Hemo-compatibility

JI Jian, FENG Lin-Xian, SHEN Jia-Cong   

  1. Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027, China
  • Received:2001-08-21 Online:2002-12-24 Published:2002-12-24

摘要: 采用125I放射标记技术研究了血浆白蛋白和纤维蛋白原在聚甲基丙烯酸甲酯-接枝-十八烷基聚氧乙烯(PMMA-g-SPEO)、聚甲基丙烯酸甲酯-接枝-乙基聚氧乙烯(PMMA-g-EPEO)和聚甲基丙烯酸甲酯-甲基丙烯酸十八酯共聚物(PMMA-co-SMA)表面的竞争吸附行为.结果表明,十八烷基聚氧乙烯复合修饰的PMMA-g-SPEO可高选择性地形成白蛋白可逆吸附层,有效地阻抗血小板的粘附,延长材料的凝血时间,是一种理想的白蛋白原位复合的生物医用功能材料.

关键词: 血液相容性, 蛋白质吸附, 原位表面修饰, 白蛋白, 纤维蛋白原

Abstract: In order to assess the hypothesis that the composite structure of srearyl group and PEO might exhibit albumin preferential adsorption by both the albumin bonding affinity of stearyl groups and the protein-resistant character of EO side chains, the adsorption of plasma proteins(fibrinogen and albumin) from buffer and plasma onto poly(methylmethacrylate-co-stearyl-methacrylate)(PMMA-co-SMA), polymethylmethacrylate)-graft-[ω-stearyl-poly(ethylene oxide)](PMMA-g-SPEO) and poly(methyl methacrylate)-graft-[ω-ethyl-poly(ethylene oxide)](PMMA-g-EPEO) was investigated by radioiodine labeling of proteins using the iodine monochloride method. The results confirm that PMMA-g-SPEO can absorb a high level of albumin and resist the fibrinogen adsorption dramatically. The surface for attracting and reversibly binding albumin, which was proved to suppress the platelet adhesion and prolong the clotting time, has been developed on the composite surface structure of srearyl group and PEO.

Key words: Blood compatibility, Protein adsorption, In-situ surface modification, Albumin, Fibrinogen

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