Supramolecular engineering of high-efficiency nanozymes via chain-length-directed crystallization of cellulose oligomers.

Nanozymes are nanomaterials designed to mimic the catalytic functions of natural enzymes, offering advantages such as enhanced stability, tunability, and scalability. Although precise control over the spatial arrangement of catalytic centers is essential for maximizing nanozyme activity, it remains a fundamental challenge in nanozyme design. Here, we present a supramolecular strategy to achieve molecular-level engineering of catalytic centers by grafting hemin onto monodisperse cellulose oligomers (MCOs). The crystallization-driven self-assembly of MCOs directs the spatial organization of hemin while preventing its detrimental aggregation. Systematically tuning of the cellulose chain length reveals that a degree of polymerization (DP) of 6 optimally balances supramolecular packing and increased availability of active sites, whereas shorter (DP1) and longer (DP20) chains compromise catalytic performance due to aggregation or decreased substrate binding affinity. Structural analyses reveal that chain-length-directed crystallization governs nanozyme morphology, aggregation behavior, and catalytic performance. Through this approach, we achieve an approximately 500-fold enhancement in catalytic efficiency over free hemin, while structural analyses elucidate the role of chain-length-dependent crystallization in governing nanozyme morphology and performance. This study establishes transferable cellulose-based supramolecular strategy for engineering high-performance nanozymes with broad applicability across diverse catalytic systems.