Interaction forces and morphology of a protein-resistant poly(ethylene glycol) layer
Interaction forces and morphology of a protein-resistant poly(ethylene glycol) layer
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DOI：
10.1529/biophysj.104.045443
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发表时间：
2005-01-01
影响因子：
3.4
通讯作者：
Spencer, ND
中科院分区：
文献类型：
--
作者：
Heuberger, M;Drobek, T;Spencer, ND
使用扩展表面力装置研究了涂有低分子量聚乙二醇（PEG）共聚物刷的抗蛋白质表面上的分子相互作用。观察到的相互作用力主要是排斥力并且接近弹性。这些链相对于弗洛里半径延伸，这与标度理论的定性预测一致。与理论比较可以确定相关量，例如刷子长度和吸附质量。基于这些结果，我们提出了吸附共聚物形态的分子模型。以高分辨率测量的表面力等温线可以检测到独特的结构力，表明聚乙二醇和水之间存在弱平衡网络——这一发现与 PEG 卓越的溶液特性相一致。 A. 的发生。新结构被解释为水诱导的聚合物构象空间的限制。这种限制与 PEG 蛋白抗性现象高度相关。蛋白质吸附需要蛋白质和 PEG 层中的构象转变，这在能量和动力学上都是不利的。
The molecular interactions on a protein-resistant surface coated with low-molecular-weight poly( ethylene glycol) (PEG) copolymer brushes are investigated using the extended surface forces apparatus. The observed interaction force is predominantly repulsive and nearly elastic. The chains are extended with respect to the Flory radius, which is in agreement with qualitative predictions of scaling theory. Comparison with theory allows the determination of relevant quantities such as brush length and adsorbed mass. Based on these results, we propose a molecular model for the adsorbed copolymer morphology. Surface-force isotherms measured at high resolution allow distinctive structural forces to be detected, suggesting the existence of a weak equilibrium network between poly( ethylene glycol) and water - a finding in accordance with the remarkable solution properties of PEG. The occurrence of a. ne structure is interpreted as a water-induced restriction of the polymer's conformational space. This restriction is highly relevant for the phenomenon of PEG protein resistance. Protein adsorption requires conformational transitions, both in the protein as well as in the PEG layer, which are energetically and kinetically unfavorable.