Protein–Foldamer Synthon Enables Precise Hybrid Architectures
A Nature Chemistry study reports a ribosome-display–selected Nanofitin that binds a biotinylated helical aromatic foldamer with about 92 nM affinity, forming a well-defined 1:1 complex whose interface (>700 Å^2) enables modular assembly of discrete and extended protein–foldamer architectures. The work demonstrates foldamer–protein dimers, two-fold protein–foldamer constructs, cyclic assemblies, and higher-order lattices, validated by X-ray, NMR, MS, and CD. This establishes aromatic foldamers as large, programmable interfaces to organize proteins with precise spatial control, opening paths to foldamer–protein nanocages and porous lattices.