Geometrical effect of 3D-memory cavity on the imprinting efficiency of transition-state analogue-built artificial hydrolases

Mathew, Dona; Thomas, Benny; Devaky, K. S.

doi:10.1007/s00289-017-2237-2

Cited by 4 publications

(3 citation statements)

References 27 publications

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“…The ability to tailor the imprinted sites with functional groups, allied with the robustness and stability of polymer materials, led to considerable research efforts to expand the catalytic applications of MIPs. Many different approaches have been explored (e.g., (non)covalent imprinting, chemical reactions) and catalytic MIPs have been prepared using analogues of substrates, transition states, or products as templates [ 64 , 65 , 66 , 67 , 68 ]. Since the first important developments, considerable advances in the field have allowed to prepare more flexible and adaptative structures [ 2 , 40 ].…”

Section: Molecular Imprinting Technologymentioning

confidence: 99%

Molecular Imprinting on Nanozymes for Sensing Applications

et al. 2021

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As part of the biomimetic enzyme field, nanomaterial-based artificial enzymes, or nanozymes, have been recognized as highly stable and low-cost alternatives to their natural counterparts. The discovery of enzyme-like activities in nanomaterials triggered a broad range of designs with various composition, size, and shape. An overview of the properties of nanozymes is given, including some examples of enzyme mimics for multiple biosensing approaches. The limitations of nanozymes regarding lack of selectivity and low catalytic efficiency may be surpassed by their easy surface modification, and it is possible to tune specific properties. From this perspective, molecularly imprinted polymers have been successfully combined with nanozymes as biomimetic receptors conferring selectivity and improving catalytic performance. Compelling works on constructing imprinted polymer layers on nanozymes to achieve enhanced catalytic efficiency and selective recognition, requisites for broad implementation in biosensing devices, are reviewed. Multimodal biomimetic enzyme-like biosensing platforms can offer additional advantages concerning responsiveness to different microenvironments and external stimuli. Ultimately, progress in biomimetic imprinted nanozymes may open new horizons in a wide range of biosensing applications.

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Section: Molecular Imprinting Technologymentioning

confidence: 99%

Molecular Imprinting on Nanozymes for Sensing Applications

et al. 2021

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“…30 Subsequently, a variety of catalytically active MIPs were synthesized by taking substrate analogs, transition states, and products or intermediates as templates. 31–35 Although the MIP-based artificial enzymes prepared by such a strategy can exhibit high catalytic activity, there are still some obstacles that limit the higher activity, including difficulties in template removal, slow transport of materials inside and outside the polymer, and most importantly, heterogeneity of binding sites leading to extensive binding affinity. 36 Therefore, it is desirable to develop suitable methods for the rational preparation of MIP-based artificial enzymes with high catalytic activity and high specific selectivity.…”

Section: Introductionmentioning

confidence: 99%

Recent development in the design of artificial enzymes through molecular imprinting technology

Tian

et al. 2022

J. Mater. Chem. B

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“…Mainly, inorganic systems and MOFs simulate the activity of oxidoreductases like peroxidase, superoxide dismutase, glucose oxidase, and catalase [6,7]. Another group of enzymes that mimic with catalytic properties is based on the introduction of catalytically active groups into the polymeric matrix [8,9]. This technique is similar to molecular imprinting, the main idea of which is a formation of highly cross-linked polymer matrix around a template [3,10].…”

Section: Introductionmentioning

confidence: 99%

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

et al. 2020

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Synthetic catalysts that could compete with enzymes in term of the catalytic efficiency but surpass them in stability have a great potential for the practical application. In this work, we have developed a novel kind of organic catalysts based on flow-through macroporous polymer monoliths containing catalytic centers that mimic the catalytic site of natural enzyme chymotrypsin. It is known that chymotrypsin catalytic center consists of L-serine, L-histidine, and L-aspartic acid and has specificity to C-terminal residues of hydrophobic amino acids (L-phenylalanine, L-tyrosine, and L-tryptophan). In this paper, we have prepared the macroporous polymer monoliths bearing grafted polymer layer on their surface. The last one was synthesized via copolymerization of N-methacryloyl-L-serine, N-methacryloyl-L-histidine, and N-methacryloyl-L-aspartic acid. The spatial orientation of amino acids in the polymer layer, generated on the surface of monolithic framework, was achieved by coordinating amino acid-polymerizable derivatives with cobalt (II) ions without substrate-mimicking template and with its use. The conditions for the preparation of mimic materials were optimized to achieve a mechanically stable system. Catalytic properties of the developed systems were evaluated towards the hydrolysis of ester bond in a low molecular substrate and compared to the results of using chymotrypsin immobilized on the surface of a similar monolithic framework. The effect of flow rate increase and temperature elevation on the hydrolysis efficiency were evaluated for both mimic monolith and column with immobilized enzyme.

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Geometrical effect of 3D-memory cavity on the imprinting efficiency of transition-state analogue-built artificial hydrolases

Cited by 4 publications

References 27 publications

Molecular Imprinting on Nanozymes for Sensing Applications

Molecular Imprinting on Nanozymes for Sensing Applications

Recent development in the design of artificial enzymes through molecular imprinting technology

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

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