Abstract
A soluble glutathione peroxidase mimic with the optimum structure (NCD-Te-NCD2.2) was constructed based on the supramolecular host-guest interaction. The self-assembled structure and catalytic mechanism of NCD-Te-NCD2.2 were detailed investigation. It was proved that NCD-Te-NCD2.2 could form the hollow vesicle-like aggregates in water. And saturation kinetics measurement indicated that NCD-Te- NCD2.2 exhibited the typical enzyme catalytic behavior. Furthermore, benefited from the hydrophobic microenvironment in vesicle-like aggregates, NCD-Te-NCD2.2 exhibited the specific recognition ability for hydrophobic substrates, which was one of the important characteristics of native glutathione peroxidase. The successful construction of NCD-Te-NCD2.2 not only provides an efficient preparation method for soluble GPx mimic but also highlights for construction of other giant supramolecular biomimetic enzymes.
Keywords: Biomimetics, enzyme activity, glutathione peroxidase, supramolecular, host-guest interaction.
Graphical Abstract
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