Yanzhen Yin, Shufei Jiao, Ruirui Zhang, Xueqian Wang, Li Zhang and Lan Yang Pages 64 - 70 ( 7 )
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.
Biomimetics, enzyme activity, glutathione peroxidase, supramolecular, host-guest interaction.
Guangxi Colleges and Universities Key Laboratory of Beibu Gulf oil and Natural Gas Resource Effective Utilization, Qinzhou University, Qinzhou 535000 China.