Protein interface redesign facilitates conversion of zero-dimensional protein nanomaterials to their one- and two-dimensional analogues
Abstract Although various artificial protein nanoarchitectures have been constructed, controlling conversion between protein assemblies with different dimensions has largely been unexplored. Here, we describe a simple, effective approach to regulate conversion between 0D protein nanomaterials and their 1D or 2D analogues by adjusting the geometric arrangement of dimeric protein building blocks. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimeric protein, twelve of which interact with each other in a head-to-side manner to generate 0D 24-meric protein nanocage in the presence of Ca2+. By tuning two contiguous dimeric proteins to interact in a fully or partially side-by-side fashion through protein interface redesign, we can render the conversion of the inherent salt-mediated 0D protein nanocage into 1D or 2D nanomaterials in response to multiple external stimuli. Thus, one kind of dimeric protein building block can generate three protein materials with different dimensions in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.