The efficiency and selectivity of enzymatic transformations have motivated the exploration of increasingly complex substrates, including glycopolymers. However, the enzymatic modification of such unconventional substrates remains underexplored. Here, we report the synthesis via RAFT polymerization of methacrylate-based linear homo- and block glycopolymers bearing pendant D-glucose units attached to the polymer backbone, with no intervening spacer. The pendant glucose moieties of the homoglycopolymers are effectively oxidized by glucose oxidase (GOx), reaching 48% conversion to gluconic acid within 24 h, consistent with a processive mechanism. Patterned block copolymers containing protected and deprotected glucose units further reveal that GOx can access pendant glucose residues whether they are located at terminal or internal positions within the polymer chain. Molecular docking studies support these observations, showing that the anomeric carbon can reach the enzyme active-site residues. These results highlight enzyme-mediated transformations as a powerful strategy for the straightforward and selective functionalization of unconventional polymeric substrates.
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Bonilla et al. (2026) studied this question.
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