Substrate chemistry-dependent conformations of single laminin molecules on polymer surfaces are revealed by the phase signal of atomic force microscopy
Substrate chemistry-dependent conformations of single laminin molecules on polymer surfaces are revealed by the phase signal of atomic force microscopy
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DOI：
10.1529/biophysj.106.102491
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发表时间：
2007-07-01
影响因子：
3.4
通讯作者：
Monleon Pradas, Manuel
中科院分区：
文献类型：
--
作者：
Carlos Rodriguez Hernandez, Jose;Salmeron Sanchez, Manuel;Monleon Pradas, Manuel
利用攻丝模式原子力显微镜（AFM）的相位大小，直接观察了单个层粘连蛋白分子吸附在合成底物上的构象。使用AFM，如果使用高度信号，则不可能区分底物上的蛋白质，因为材料的粗糙度与吸附的蛋白质具有相同的数量级，通常为10nm高度。这项工作显示了AFM如何被利用来揭示聚合物材料上的蛋白质构象。在一系列基于丙烯酸乙酯和丙烯酸羟乙酯的不同共聚物上观察到不同的层粘连蛋白形态作为- oh基团表面密度的函数：从球形到完全扩展的蛋白质分子形态得到，并且可以清楚地识别一些底物上层粘连蛋白网络形成的开始。结果强调了潜在的合成底物的表面化学对吸附蛋白质的生物功能构象的重要性。
The conformation of single laminin molecules adsorbed on synthetic substrates is directly observed making use of the phase magnitude in tapping mode atomic force microscopy (AFM). With AFM, it is not possible to differentiate the proteins on the substrate if use is made of the height signal, since the roughness of the material becomes of the same order of magnitude as the adsorbed protein, typically 10 nm height. This work shows how AFM can be exploited to reveal protein conformation on polymer materials. Different laminin morphologies are observed on a series of different copolymers based on ethyl acrylate and hydroxyethyl acrylate as a function of the surface density of -OHgroups: from globular to completely extended morphologies of the protein molecules are obtained, and the onset of laminin network formation on some substrates can be clearly identified. The results stress the importance of the underlying synthetic substrate's surface chemistry for the biofunctional conformation of adsorbed proteins.