Protein interface redesign facilitates the transformation of nanocage building blocks to 1D and 2D nanomaterials.

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, nan

SUBMITTER: Zhang X 

PROVIDER: S-EPMC8357837 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature