Distinctive Adsorption Mechanism and Kinetics of Immunoglobulin G on a Nanoscale Polymer Surface
Distinctive Adsorption Mechanism and Kinetics of Immunoglobulin G on a Nanoscale Polymer Surface
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免疫球蛋白 G 在纳米级聚合物表面的独特吸附机制和动力学
DOI：
10.1021/acs.langmuir.1c02710
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发表时间：
2022
期刊：
影响因子：
3.9
通讯作者：
Hahm, Jong-in
中科院分区：
文献类型：
--
作者：
Cho, David H.;Xie, Tian;Mulcahey, Patrick J.;Kelleher, Noah P.;Hahm, Jong-in
阐明蛋白质从简单的聚合物表面吸附到具有更大化学复杂性和纳米级特征的聚合物表面，对于开发控制良好的纳米生物材料和纳米生物传感器至关重要。在本研究中，我们反复忠实地跟踪嵌段共聚物（BCP）表面相同纳米区域上的单个蛋白质，并监测模型蛋白免疫球蛋白G （IgG）随时间的吸附和组装行为，从而形成紧密的表面填充结构。由于在生物分子水平上可以清楚地看到离散的蛋白质吸附事件，因此，IgG在BCP纳米结构域表面的详细组装和包装状态随后与IgG吸附动力学图的各种机制相关。有趣的是，从宏观均聚物模板中观察到的特征完全不同，从纳米尺度的IgG吸附等温线中发现，化学变化的BCP表面。它们包括两个langmuir类吸附段的存在和吸附图中的非单调状态。通过与时间对应的地形数据的关联，可以用BCP上IgG吸附途径的单生物分子水平细节来解释独特的等温线特征。这项工作不仅为纳米级聚合物表面上的时间分辨、单蛋白水平的吸附事件提供了急需的直接实验证据，而且还表明了蛋白质吸附的特定形貌状态与吸附等温线特定部分的组装之间的相互联系。从基础研究的角度来看，研究单个蛋白质的纳米级表面组织及其局部和全局吸附动力学曲线的相关能力对于准确确定蛋白质组装机制和解释蛋白质在纳米级表面的吸附动力学具有重要价值。应用方面，这些知识对于从根本上指导利用纳米级聚合物结构的生物材料和生物医学设备的设计和开发也很重要。
Elucidation of protein adsorption beyond simple polymer surfaces to those presenting greater chemical complexity and nanoscopic features is critical to developing well-controlled nanobiomaterials and nanobiosensors. In this study, we repeatedly and faithfully track individual proteins on the same nanodomain areas of a block copolymer (BCP) surface and monitor the adsorption and assembly behavior of a model protein, immunoglobulin G (IgG), over time into a tight surface-packed structure. With discrete protein adsorption events unambiguously visualized at the biomolecular level, the detailed assembly and packing states of IgG on the BCP nanodomain surface are subsequently correlated to various regimes of IgG adsorption kinetic plots. Intriguing features, entirely different from those observed from macroscopic homopolymer templates, are identified from the IgG adsorption isotherms on the nanoscale, chemically varying BCP surface. They include the presence of two Langmuir-like adsorption segments and a nonmonotonic regime in the adsorption plot. Via correlation to time-corresponding topographic data, the unique isotherm features are explained with single biomolecule level details of the IgG adsorption pathway on the BCP. This work not only provides much needed, direct experimental evidence for time-resolved, single protein level, adsorption events on nanoscale polymer surfaces but also signifies mutual linking between specific topographic states of protein adsorption and assembly to particular segments of adsorption isotherms. From the fundamental research viewpoint, the correlative ability to examine the nanoscopic surface organizations of individual proteins and their local as well as global adsorption kinetic profiles will be highly valuable for accurately determining protein assembly mechanisms and interpreting protein adsorption kinetics on nanoscale surfaces. Application-wise, such knowledge will also be important for fundamentally guiding the design and development of biomaterials and biomedical devices that exploit nanoscale polymer architectures.