Shape and Size Complementarity-Induced Formation of Supramolecular Protein Assemblies with Metal-Oxo Clusters

Abstract

The controlled formation of protein supramolecular assemblies is challenging, but it could provide an important route for the development of hybrid biomaterials. In this work, we demonstrate the formation of well-defined complexes between the eightfold symmetrical designer protein Tako8 and soluble metal-oxo clusters from the family of Anderson–Evans, Keggin, and ZrIV-substituted Wells–Dawson polyoxometalates. A combination of X-ray crystallography and solution studies showed that metal-oxo clusters are able to serve as linker nodes for the bottom-up creation of protein-based supramolecular assemblies. Our findings indicate that clusters with larger size and negative charge are capable of modulating the crystal packing of the protein, highlighting the need for a size and shape complementarity with the protein node for optimal alteration of the crystalline self-assembly.