Engineering surface amphiphilicity of polymer nanostructures. (January 2022)

• Record Type: Journal Article
• Authors: Xiang, Siyuan; Hammer, Brenton; Kremer, Kurt; Müllen, Klaus; Weil, Tanja
• Is Part Of: Progress in polymer science. Volume 124(2022)
• Publication Date: 2022-01
• Subjects: Amphiphilic surface structures -- Protein-like molecules -- Striped metal nanoparticles -- Polyphenylene dendrimers -- Cell uptake -- Protein corona; Polymers -- Periodicals; Polymerization -- Periodicals; Polymers -- Industrial applications -- Periodicals; Polymères -- Périodiques; Polymérisation -- Périodiques; 547.7
• DOI: 10.1016/j.progpolymsci.2021.101489
• Languages: English
• ISSNs: 0079-6700

Abstract

Abstract: 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 in 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. Graphical abstract: Image, graphical abstract