Multivalent‐Interaction‐Driven Assembly of Discrete, Flexible, and Asymmetric Supramolecular Protein Nano‐Prisms

Abstract

Current approaches to design monodisperse protein assemblies require rigid, tight, and symmetric interactions between oligomeric protein units.H erein, we introduce an ew multivalent-interaction-driven assembly strategy that allows flexible,s paced, and asymmetric assembly between protein oligomers.Wediscoveredthat two polygonal protein oligomers (ranging from triangle to hexagon) dominantly form adiscrete and stable two-layered protein prism nanostructure via multivalent interactions between fused binding pairs.W ed emonstrated that protein nano-prisms with long flexible peptide linkers (over 80 amino acids) between protein oligomer layers could be discretely formed. Oligomers with different structures could also be monodispersely assembled into two-layered but asymmetric protein nano-prisms.F urthermore,p roducing higher-order architectures with multiple oligomer layers,f or example,3-layeredn ano-prisms or nanotubes,w as also feasible.