Molecular Imprinting for Substrate Selectivity and Enhanced Activity of Enzyme Mimics

Small ◽  
2016 ◽  
Vol 13 (7) ◽  
pp. 1602730 ◽  
Author(s):  
Zijie Zhang ◽  
Biwu Liu ◽  
Juewen Liu
Soft Matter ◽  
2020 ◽  
Vol 16 (30) ◽  
pp. 7033-7039 ◽  
Author(s):  
Jingyi Li ◽  
Mingjie Zhu ◽  
Mengfan Wang ◽  
Wei Qi ◽  
Rongxin Su ◽  
...  

Peroxidase (POD)-mimicking catalysts with enhanced activity and specificity were constructed based on the strategy of peptide assembly and molecular imprinting.


2019 ◽  
Vol 11 (36) ◽  
pp. 4586-4592 ◽  
Author(s):  
Fan Lin ◽  
Tian Yushen ◽  
Lou Doudou ◽  
Wu Haoan ◽  
Cui Yan ◽  
...  

Based on the research of the oxidase-like activity of various Au-based nanostructures, a novel AuPtNPs based GOD mimic with substrate-selectivity and an enhanced catalytic activity was constructed by molecular imprinting technology.


2018 ◽  
Vol 5 (4) ◽  
pp. 738-744 ◽  
Author(s):  
Zijie Zhang ◽  
Juewen Liu

Molecular imprinting of enzyme mimics allows delivery and selective catalysis and protection of the enzyme in cells.


2020 ◽  
Vol 65 (1) ◽  
pp. 28-41
Author(s):  
Marwa Aly Ahmed ◽  
Júlia Erdőssy ◽  
Viola Horváth

Multifunctional nanoparticles have been shown earlier to bind certain proteins with high affinity and the binding affinity could be enhanced by molecular imprinting of the target protein. In this work different initiator systems were used and compared during the synthesis of poly (N-isopropylacrylamide-co-acrylic acid-co-N-tert-butylacrylamide) nanoparticles with respect to their future applicability in molecular imprinting of lysozyme. The decomposition of ammonium persulfate initiator was initiated either thermally at 60 °C or by using redox activators, namely tetramethylethylenediamine or sodium bisulfite at low temperatures. Morphology differences in the resulting nanoparticles have been revealed using scanning electron microscopy and dynamic light scattering. During polymerization the conversion of each monomer was followed in time. Striking differences were demonstrated in the incorporation rate of acrylic acid between the tetramethylethylenediamine catalyzed initiation and the other systems. This led to a completely different nanoparticle microstructure the consequence of which was the distinctly lower lysozyme binding affinity. On the contrary, the use of sodium bisulfite activation resulted in similar nanoparticle structural homogeneity and protein binding affinity as the thermal initiation.


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