Aggregation behavior and interaction with human serum albumin of 2-oxazoline block copolymers in aqueous solutions
Aggregation behavior and interaction with human serum albumin of 2-oxazoline block copolymers in aqueous solutions
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DOI：
10.1002/macp.1997.021980109
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发表时间：
1997-01-01
影响因子：
2.5
通讯作者：
Maeda, S
中科院分区：
文献类型：
--
作者：
Naka, K;Nakamura, T;Maeda, S
用尺寸排阻色谱、动态光散射和透射电子显微镜研究了以聚N-乙酰亚胺乙烯为亲水嵌段、聚N-乙酰亚胺乙烯为疏水嵌段的嵌段共聚物聚集体的结构。由球形和棒状胶束组成的聚集体的形态取决于嵌段共聚物的化学结构。采用体积排阻色谱法研究了不同聚合物聚集体对人血清白蛋白（HSA）的吸附行为。结合到聚合物聚集体上的HSA的最大量取决于聚合物聚集体的形态。HSA对每种聚合物聚集体的吸附等温线与Langmuir吸附等温线吻合良好。吸附到聚集体上的HSA的量不受HSA中脂肪酸含量的影响。没有HSA的聚集体的电泳迁移率接近于零，并且当HSA掺入到聚集体中时，负迁移率增加。实验结果表明，吸附HSA的聚集体主要发生在表面或在亲水壳的聚合物聚集体，而不是在疏水的聚合物胶束的核心。
The structure of the aggregates of block copolymers containing poly[(N-acetylimino)ethylene] as hydrophilic block and poly[(N-acylimino)ethylene]s as hydrophobic block was studied by size exclusion chromatography, dynamic light scattering, and transmission electron microscopy. The morphology of the aggregates, consisting of spherical and rod-like micelles, depends on the chemical structure of the block copolymers. The adsorption behavior of human serum albumin (HSA) onto each polymer aggregate was studied by size exclusion chromatography. The maximum amount of HSA bound onto the polymer aggregates depends on the morphology of the polymer aggregates. Adsorption isotherms of HSA for each polymer aggregate are in good agreement with a Langmuir adsorption isotherm. The amount of HSA adsorbed onto the aggregates is not influenced by the fatty acid content in HSA. The electrophoretic mobility of the aggregates without HSA is close to zero, and the negative mobility increases when HSA is incorporated into the aggregates. The experimental results suggest that adsorption of HSA to the aggregates occurs mainly at the surface or at the hydrophilic shell of the polymer aggregates, not at the hydrophobic core of the polymer micelles.