Suppression of protein adsorption on a charged phospholipid polymer interface.
Suppression of protein adsorption on a charged phospholipid polymer interface.
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DOI：
10.1021/bm801279y
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发表时间：
2009-02
影响因子：
6.2
通讯作者：
Yan Xu;M. Takai;K. Ishihara
中科院分区：
文献类型：
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作者：
Yan Xu;M. Takai;K. Ishihara
据报道，带电界面具有抑制阴离子和阳离子蛋白质吸附的高能力。该界面通过阴离子磷脂共聚物聚(2-甲基丙烯酰氧基乙基磷酰胆碱(MPC)-共-甲基丙烯酸正丁酯(BMA)-共-3-甲基丙烯酰氧基丙基磺酸钾(PMPS)-共-3-甲基丙烯酰氧基丙基三甲氧基硅烷(MPTMSi))(PMBSSi)共价构建在石英上。 PMBSSi界面非常亲水且均匀，即使在长期流体工作条件下也能长期有效地发挥作用。界面上的PMBSSi密度可以通过调节改性溶液的PMBSSi浓度来控制，影响表面特性，包括表面接触角、表面粗糙度和表面zeta电位。当应用 PMBSSi 改性时，各种蛋白质（等电点从 1.0 到 11.0 不等）在石英上的吸附量减少到至少 87%，尽管这些蛋白质具有各种电性质。 PMBSSi 界面上的蛋白质吸附行为更多地取决于 PMBSSi 密度而不是表面电荷。 PMBSSi 修饰不仅在生理离子强度上，而且在一定范围的离子强度上对表面都有稳定的影响，这表明静电相互作用并不主导蛋白质吸附到 PMBSSi 表面的行为。
High capability of a charged interface to suppress adsorption of both anionic and cationic proteins was reported. The interface was covalently constructed on quartz by modifying with an anionic phospholipid copolymer, poly(2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA)-co-potassium 3-methacryloyloxypropyl sulfonate (PMPS)-co-3-methacryloxypropyl trimethoxysilane (MPTMSi)) (PMBSSi). The PMBSSi interfaces were very hydrophilic and homogeneous and could function effectively for a long time even under long-term fluidic working conditions. The PMBSSi density on the interface, which was controllable by adjusting the PMBSSi concentration of the modification solution, affected the surface properties, including the surface contact angle, the surface roughness, and the surface zeta-potential. When a PMBSSi modification was applied, the adsorption of various proteins (isoelectric point varying from 1.0 to 11.0) on quartz was reduced to at least 87% in amount, despite the various electrical natures these proteins have. The protein adsorption behavior on the PMBSSi interface depended more on the PMBSSi density than on the surface charge. The PMBSSi modification had a stable impact on the surface, not only at the physiologic ionic strength, but also over a range of the ionic strength, suggesting that electrostatic interactions do not dominate the behavior of protein adsorption to the PMBSSi surface.