Abstract
Although various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Here, we describe an approach to realize the self-assembly transformation of dimeric building blocks by adjusting their geometric arrangement. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer; twelve of these dimers interact with each other in a head-to-side manner to generate 24-meric hollow protein nanocage in the presence of Ca2+ or PEG. 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 self-assembly transformation of such dimeric building blocks from the protein nanocage to filament, nanorod and nanoribbon in response to multiple external stimuli. We show similar dimeric protein building blocks can generate three kinds of protein materials in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.
Highlights
Various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored
The four helix bundle structure, which is widely distributed in Nature, has been utilized as building blocks to construct a number of proteins and enzymes to perform a considerably wide range of functions, such as iron storage by ferritin[26], DNA protection by Dps protein[27], copper storage by Csp[142], electron transfer by cytochrome cb56243, ribonucleotide reduced into deoxynucleotide by R2 subunit of ribonucleotide reductase[44], methane oxidized into methanol by methane monooxygenase[45], and so on
Four helix bundles are attractive for synthetic chemists because its interfaces are dominated by side chain and side chain interactions, which can be more tunable than βstrands
Summary
Various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Different strategies such as de novo design[32,33,34], fusion protein[14,35,36], directed evolution[37,38,39], and key interface redesign[40,41] have been built to create a variety of artificial hollow protein nanocages that rival the size, property, and functionality of their natural analogs Despite these advances, rendering PPIs controllable to facilitate the transformation of the building blocks from protein nanocages into 1D or high-order nanomaterials in the laboratory has yet to be explored. This approach opens up an avenue for constructing 1D or 2D nanoarchitectures with the building blocks of hollow protein nanocage as starting materials
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