Direct synthesis of molecularly imprinted nanozymes with a biomimetic catalytic motif for glycosidic bond cleavage

2026-08-11

ML Mohan Lakavathu

Yan Zhao *

DOI：10.3389/fchem.2026.1866827

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Carbohydrates are the most abundant organic molecules on Earth and play essential roles in biology. Natural glycosidases cleave glycosidic linkages using a pair of conserved carboxylic acid residues. Here we report the direct synthesis of nanozymes that mimic glycosidases through molecular imprinting of thiosemicarbazide-derived glycan templates; prepared in one step from unprotected mono- or oligosaccharides. The thiosemicarbazide group binds strongly to a dicarboxylic acid functional monomer (FM); enabling installation of the double-acid catalytic motif into the imprinted active site. The resulting nanozymes cleave glycosidic bonds in oligo- and polysaccharides (e.g.; cellobiose and cellulose) by a mechanism analogous to retaining glycosidases. Molecular imprinting also allows the active site to accommodate a single or predefined number of sugar residues; tuning both the size of the pocket and the distance between binding and catalytic groups; thereby enabling rational control of the cleavage site along the substrate.

Keywords:

cellulose

micelle

molecular imprinting

artificial enzyme

biomass conversion

cross-linking

Direct synthesis of molecularly imprinted nanozymes with a biomimetic catalytic motif for glycosidic bond cleavage

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