Double‐Layered Supramolecular Prisms Self‐Assembled by Geometrically Non‐equivalent Tetratopic Subunits

Abstract Supramolecular cages/vesicles in biology display sophisticated structures and functions by utilizing a few types of protein subunit quasi‐equivalently at distinct geometrical locations. However, synthetic supramolecular cages still lack comparable complexity to reach the high levels of functionality found in natural systems. Herein we report the self‐assembly of giant pentagonal supramolecular prisms (molecular weight >50 kDa) with tetratopic pyridinyl subunits serving different geometrical roles within the structures, and their packing into a novel superstructure with unexpected three‐fold rotational symmetry in a single two‐dimensional layer of crystalline state. The formation of these complicated structures is controlled by both the predetermined angles of the ligands and the mismatched structural tensions created from the multi‐layered geometry of the building blocks. Such a self‐assembly strategy is extensively used by viruses to increase the volume and complexity of capsids and would provide a new approach to construct highly sophisticated supramolecular architectures.