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- W4200504742 endingPage "101489" @default.
- W4200504742 startingPage "101489" @default.
- W4200504742 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." @default.
- W4200504742 created "2021-12-31" @default.
- W4200504742 creator A5003379329 @default.
- W4200504742 creator A5045919949 @default.
- W4200504742 creator A5054881563 @default.
- W4200504742 creator A5072097825 @default.
- W4200504742 creator A5078466092 @default.
- W4200504742 date "2022-01-01" @default.
- W4200504742 modified "2023-10-18" @default.
- W4200504742 title "Engineering surface amphiphilicity of polymer nanostructures" @default.
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