scholarly journals Molecular Recognition of Enzymes and Modulation of Enzymatic Activity by Nanoparticle Conformational Sensors

2022 ◽  
Author(s):  
Kaiqian Chen ◽  
Yan Zhao

Regulation of enzyme activity is key to dynamic processes in biology but is difficult to achieve with synthetic systems. We here report molecularly imprinted nanoparticles with strong binding for the...

RSC Advances ◽  
2021 ◽  
Vol 11 (13) ◽  
pp. 7732-7737
Author(s):  
Fenying Wang ◽  
Dan Wang ◽  
Tingting Wang ◽  
Yu Jin ◽  
Baoping Ling ◽  
...  

Fluorescent molecularly imprinted polymer (FMIP) gains great attention in many fields due to their low cost, good biocompatibility and low toxicity. Here, a high-performance FMIP was prepared based on the autocatalytic silica sol–gel reaction.


Sensors ◽  
2021 ◽  
Vol 21 (8) ◽  
pp. 2757
Author(s):  
W. Rudolf Seitz ◽  
Casey J. Grenier ◽  
John R. Csoros ◽  
Rongfang Yang ◽  
Tianyu Ren

This perspective presents an overview of approaches to the preparation of molecular recognition agents for chemical sensing. These approaches include chemical synthesis, using catalysts from biological systems, partitioning, aptamers, antibodies and molecularly imprinted polymers. The latter three approaches are general in that they can be applied with a large number of analytes, both proteins and smaller molecules like drugs and hormones. Aptamers and antibodies bind analytes rapidly while molecularly imprinted polymers bind much more slowly. Most molecularly imprinted polymers, formed by polymerizing in the presence of a template, contain a high level of covalent crosslinker that causes the polymer to form a separate phase. This results in a material that is rigid with low affinity for analyte and slow binding kinetics. Our approach to templating is to use predominantly or exclusively noncovalent crosslinks. This results in soluble templated polymers that bind analyte rapidly with high affinity. The biggest challenge of this approach is that the chains are tangled when the templated polymer is dissolved in water, blocking access to binding sites.


2006 ◽  
Vol 571 (2) ◽  
pp. 235-241 ◽  
Author(s):  
Xiangjun Liu ◽  
Canbin Ouyang ◽  
Rui Zhao ◽  
Dihua Shangguan ◽  
Yi Chen ◽  
...  

Polymer ◽  
2006 ◽  
Vol 47 (11) ◽  
pp. 3792-3798 ◽  
Author(s):  
Li-Qin Lin ◽  
Ying-Chun Li ◽  
Qiang Fu ◽  
Lang-Chong He ◽  
Jing Zhang ◽  
...  

2003 ◽  
Vol 143 (2-3) ◽  
pp. 155-162 ◽  
Author(s):  
Hiroshi Shiigi ◽  
Hidetaka Yakabe ◽  
Masayoshi Kishimoto ◽  
Daisuke Kijima ◽  
Yuan Zhang ◽  
...  

Genetics ◽  
1980 ◽  
Vol 94 (2) ◽  
pp. 327-339 ◽  
Author(s):  
Richard Snow

ABSTRACT The HIS1 and THR4 loci are the structural genes for phosphoribosyl-ATP pyrophosphorylase and threonine synthetase, respectively. The allele his1-IS has no enzyme activity at 30", but does have activity at 15" provided the cell contains the wild-type THR4 allele or a suppressing allele at another locus, designated SUP(his1-1S). Under these conditions, cells with the hisl-IS mutation are capable of growth on minimal medium at 15". Three kinds of reversions of a hisl-IS thr4 sup(his1-IS) strain to histidine prototrophy have been obtained: (1) his1-IS locus reversions to HIS1 that restore growth without added histidine at 30", (2)  thr4 reversions to THR4 that simultaneously eliminate the requirement for threonine and restore the low-temperature effect on the his1-IS allele, and (3)mutations from sup to SUP. The SUP allele is not an ochre suppressor, and it is not linked to either HISI, THR4 or a centromere. It may represent a missense suppressor. I t is proposed that the effect ofTHR4 is caused by aggregation of the wild-type threonine synthetase with defective his1-IS monomers, causing a favorable conformational change in the histidine protein that restores limited enzymatic activity. This can be regarded as a case of complementation between nonhomologous proteins.


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