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Engineering Surface Amphiphilicity of Polymer Nanostructures
Progress in Polymer Science ( IF 27.1 ) Pub Date : 2021-12-02 , DOI: 10.1016/j.progpolymsci.2021.101489
Siyuan Xiang 1, 2 , Brenton Hammer 1 , Kurt Kremer 1 , Klaus Müllen 1 , Tanja Weil 1
Affiliation  

Surface amphiphilicity plays an important role in many important biological processes such as protein folding, protein-protein interactions as well as the formation of ordered protein nanostructures like virus capsids, protein fibers or protein networks. Still, there is a lack of understanding how the distribution of polar-nonpolar surface structures and ultimately the formation of ordered amphiphilic topologies will affect their interaction with biological amphiphiles such as lipid bilayers, cell membranes, proteins or higher ordered protein nanostructures. Herein, we will first summarize different synthesis strategies to control the formation of colloidal stable synthetic nanostructures with amphiphilic surface groups. Important examples include metal nanoparticles with ordered distributions of their polar-nonpolar surface ligands as well as aliphatic and polyphenylene dendrimers, where the surface end groups have been attached with molecular definition. Different characterization techniques that allow studying amphiphilic nanostructures in solution as well as on surfaces will be highlighted. We will also present current state-of-the art knowledge about their interactions with biological amphiphiles such as lipid bilayers, cell membranes and proteins to shed light on the impact of ordered polar-non-polar surface topologies complex biological processes. In selected examples, we will showcase amphiphilic surface structures with unexpected features in biological environments such as more efficient membrane uptake, high binding specificity to virions or the capacity to disassemble already formed peptide nanostructures. These unique characteristics will open new perspectives for designing next-generation drug delivery systems and improved viral gene delivery vectors.



中文翻译:

聚合物纳米结构的工程表面两亲性

表面两亲性在许多重要的生物过程中起着重要作用,例如蛋白质折叠、蛋白质-蛋白质相互作用以及有序蛋白质纳米结构(如病毒衣壳、蛋白质纤维或蛋白质网络)的形成。尽管如此,仍然缺乏了解极性 - 非极性表面结构的分布以及最终有序两亲拓扑的形成将如何影响它们与生物两亲分子(如脂质双层、细胞膜、蛋白质或更高有序的蛋白质纳米结构)的相互作用。在此,我们将首先总结不同的合成策略,以控制具有两亲性表面基团的胶体稳定合成纳米结构的形成。重要的例子包括具有有序分布的极性-非极性表面配体的金属纳米粒子以及脂肪族和聚亚苯基树枝状聚合物,其中表面端基已通过分子定义连接。将强调允许研究溶液中和表面上的两亲纳米结构的不同表征技术。我们还将展示有关它们与生物两亲物(如脂质双层、细胞膜和蛋白质)相互作用的最新知识,以阐明有序极性-非极性表面拓扑复杂生物过程的影响。在选定的例子中,我们将展示在生物环境中具有意想不到的特征的两亲表面结构,例如更有效的膜吸收,对病毒粒子的高结合特异性或分解已经形成的肽纳米结构的能力。这些独特的特性将为设计下一代药物递送系统和改进的病毒基因递送载体开辟新的视角。

更新日期:2021-12-02
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