Year: 2026
Type: article
Abstract: Constructing artificial assemblies that combine proteins and synthetic ligands has been hampered by the lack of protein-ligand interfaces that are sufficiently large and organized to enable precise structural control. Here ribosome display selection is used to identify a protein that binds a helical aromatic foldamer both tightly and selectively through a sizeable surface area. We used this complex as a supramolecular synthon to create well-defined hybrid foldamer-protein architectures. Examples include foldamers that bind two proteins and hold them at a precise distance, proteins that bind two foldamers and crystals in which proteins and foldamers are connected in cyclic or infinite arrays. The modularity of aromatic foldamers brings a further dimension to protein-based assemblies.
Source: Nature Chemistry
Institutions: Ludwig-Maximilians-Universität München, Centre National de la Recherche Scientifique, Université de Bordeaux, Chimie et Biologie des Membranes et des Nanoobjects, Institut Polytechnique de Bordeaux, Inserm, Acides nucléiques: Régulations naturelles et artificielles, Fritz Haber Institute of the Max Planck Society, Freie Universität Berlin, Chung-Ang University
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $12,690
Funders: European Molecular Biology Laboratory, Australian Government, Deutsche Forschungsgemeinschaft, Institut National de la Santé et de la Recherche Médicale, Centre National de la Recherche Scientifique, Ludwig-Maximilians-Universität München, Freie Universität Berlin, Deutsches Elektronen-Synchrotron
Awards: G3735907762, G4169365811, G653163216
OpenAlex ID: W7203639372