Precise spatial arrangement of catalytic centers is essential to emulate the efficiency of natural enzymatic cascades. Herein, we report a protein-mediated interfacial self-assembly strategy to construct vesicle-like proteinosomes with spatially arranged gold clusterzymes (AuNEs) to enhance multienzyme cascade catalysis. AuNEs were synthesized in situ within the confined cavity of a stable cyclic SP1 protein scaffold, genetically engineered with a Cysteine-Cysteine-Tyrosine (CCY) peptide to control cluster nucleation and growth. Metal doping with copper (Cu) and cadmium (Cd) yielded catalytically distinct Au-CuNEs and Au-CdNEs, exhibiting superoxide dismutase (SOD), glutathione peroxidase (GPx), and catalase (CAT)-like activities. These functionally complementary clusterzymes coassembled into size-tunable, ordered proteinosomes via electrostatic interactions with cetyltrimethylammonium bromide, enabling dense catalytic packing and proximity-enhanced reactions. The resulting proteinosomes displayed efficient cellular uptake and significantly improved reactive oxygen species (ROS) scavenging in Caenorhabditis elegans. This work presents a spatially programmable platform for synergistic catalysis, offering a promising approach for treating ROS-related diseases.
Hao et al. (Tue,) studied this question.
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