[3P-29] Rebuilding and altering ring-type assembly of peroxiredoxin by chemical modification
The quaternary structure (QS) of proteins is generated through specific supramolecular interactions among protein domains. Direct control of protein QS is challenging owing to the complexity of protein structure. As a protein with a characteristic QS, peroxiredoxin (Prx) from Aeropyrum pernix K1 (ApPrx) forms a ring-type decamer via the assembly of five dimers. In this work, we achieved the control of ApPrx QS assembly via amino acid mutations and chemical modifications targeting hot spots for protein assembly. The decameric QS of an ApPrx was destructed to dimers via an F80C mutation destructing the hydrophobic interactions. The dimeric ApPrxF80C mutant was then modified with small molecules and successfully assembled as a decamer by modifying the protein with a naphthalene derivative. Structural analysis confirmed that an artificially installed chemical moiety facilitates suitable protein-protein interactions to rebuild a native structure. Also, our recent results on the alteration of Prx assembly, achieved by chemical modification, will be presented. This study demonstrated that chemical modification could regulate and alter protein assembly by providing new-to-nature structural repertoire.