Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.

ABSTRACT: Protein design for self-assembly allows us to explore the emergence of protein-protein interfaces through various chemical interactions. Heterooligomers, unlike homooligomers, inherently offer a comprehensive range of structural and functional variations. Besides, the macromolecular repertoire and their applications would significantly expand if protein components could be easily interchangeable. This study demonstrates that a rationally designed bifunctional linker containing an enzyme inhibitor and maleimide can guide the formation of diverse protein heterooligomers in an easily applicable and exchangeable manner without extensive sequence optimizations. As proof of concept, we selected four structurally and functionally unrelated proteins, carbonic anhydrase, aldolase, acetyltransferase

SUBMITTER: Son S 

PROVIDER: S-EPMC10882485 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature