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.
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