In situ studies on protein adsorption onto a poly(2-methoxyethylacrylate)surface by a quartz crystal microbalance
In situ studies on protein adsorption onto a poly(2-methoxyethylacrylate)surface by a quartz crystal microbalance
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DOI：
10.1016/s0927-7757(01)00682-3
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发表时间：
2001-12
期刊：
影响因子：
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通讯作者：
Masaru Tanaka;A. Mochizuki;T. Motomura;K. Shimura;M. Onishi;Y. Okahata
中科院分区：
文献类型：
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作者：
Masaru Tanaka;A. Mochizuki;T. Motomura;K. Shimura;M. Onishi;Y. Okahata
聚（丙烯酸2-甲氧基乙酯）（PMEA）虽然化学结构简单，但却显示出良好的血液相容性，并一直致力于阐明其血液相容性的原因。众所周知，蛋白质的吸附行为影响相容性。因此，以聚甲基丙烯酸羟乙酯（PHEMA）和聚丙烯（PP）为亲水性和疏水性聚合物的代表，采用石英晶体微天平（QCM）研究了牛血清白蛋白（BSA）和人纤维蛋白原在PMEA、PHEMA和PP表面的吸附行为。根据Langmuir吸附等温线，观察到这两种蛋白质吸附到所有的聚合物表面上。从等温线得到的最大吸附量和蛋白质的表观缔合常数的PMEA低于PHEMA和PP。这些结果表明，PMEA与蛋白质之间的相互作用弱于与PP和PHEMA的相互作用。
We have reported that poly(2-methoxyethylacrylate) (PMEA) showed excellent blood compatibility though it had a simple chemical structure, and have been making efforts to clarify the reason for the blood compatibility. It is well-known that the adsorption behavior of the protein affects the compatibility. Therefore, the adsorption behaviors of bovine serum albumin (BSA) and human fibrinogen onto the surfaces of PMEA, poly(2-hydroxyethyl methacrylate) (PHEMA) and polypropylene (PP) were investigated by using a quartz crystal microbalance (QCM), where PHEMA and PP were selected as the representatives of hydrophilic and hydrophobic polymers, respectively. Both proteins were observed to adsorb onto all the polymer surfaces according to Langmuir's adsorption isotherm. The maximum adsorption amounts and the apparent association constants of the proteins for PMEA obtained from the isotherm were lower than those for PHEMA and PP. These results suggest that the interaction between PMEA and the proteins is weaker than the interaction with PP and PHEMA.