Amidase activity of phosphonate TSA-built polymer catalysts derived from organic monomers in the amidolysis of amino acid p-nitroanilides

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

doi:10.1016/j.apcata.2016.09.020

Cited by 11 publications

(5 citation statements)

References 32 publications

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“…MIPs using phosphonate templates have been developed using copolymerization and pendant grafting to polymers, providing excellent control over the internal environment of the final cross-linked product. , Again, modest esterolytic rate enhancements are observed for many of the phosphonate-templated materials (5–10 fold above background). However, more challenging amidolysis reactions and substrates such as cholesterol derivatives have been successfully catalyzed using this technology. − …”

Section: Mimicking Hydrolytic Enzymesmentioning

confidence: 99%

Synthetic Catalysts Inspired by Hydrolytic Enzymes

et al. 2018

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Enzymes, as nature’s catalysts, speed up the very reactions that make life possible. Hydrolytic enzymes are a particularly important enzyme class responsible for the catalytic breakdown of lipids, starches, and proteins in nature, and they are displaying increasing industrial relevance. While the unrivalled catalytic effect of enzymes continues to be unmatched by synthetic systems, recent progress has been made in the design of hydrolase-inspired catalysts by imitating and incorporating specific features observed in native enzyme protein structures. The development of such enzyme-inspired materials holds promise for more robust and industrially relevant alternatives to enzymatic catalysis, as well as deeper insights into the function of native enzymes. This Review will explore recent research in the development of synthetic catalysts based on the chemistry of hydrolytic enzymes. A focus on the key aspects of hydrolytic enzyme structure and catalytic mechanism will be exploredincluding active-site chemistry, tuning transition-state interactions, and establishing reactive nanoenvironments conducive to attracting, binding, and releasing target molecules. A key focus is to highlight the progress toward an effective, versatile hydrolase-inspired catalyst by incorporating the molecular design principles laid down by nature.

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Section: Mimicking Hydrolytic Enzymesmentioning

confidence: 99%

Synthetic Catalysts Inspired by Hydrolytic Enzymes

et al. 2018

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“…An attempt to directly correlate the research results with literature data is quite difficult. This is due to the incompatibility of catalytic structures with other synzymes with peptidic active fragment [44,45,46,47,48,49,50]. The comparison of the effectiveness of N -lipidated peptides immobilized on cellulose to catalyse the hydrolysis of esters [40,41] and amides indicates that degradation of amide/peptide bond is more demanding and possible only with highly active catalytic systems.…”

Section: Resultsmentioning

confidence: 99%

N-Lipidated Amino Acids and Peptides Immobilized on Cellulose Able to Split Amide Bonds

Frączyk

Kamiński

2019

Materials

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N-lipidated short peptides and amino acids immobilized on the cellulose were used ascatalysts cleaved amide bonds under biomimetic conditions. In order to select catalytically mostactive derivatives a library of 156 N-lipidated amino acids, dipeptides and tripeptides immobilizedon cellulose was obtained. The library was synthesized from serine, histidine and glutamic acidpeptides N-acylated with heptanoic, octanoic, hexadecanoic and (E)-octadec-9-enoic acids.Catalytic efficiency was monitored by spectrophotometric determination of p-nitroaniline formedby the hydrolysis of a 0.1 M solution of Z-Leu-NP. The most active 8 structures contained tripeptidefragment with 1-3 serine residues. It has been found that incorporation of metal ions into catalyticpockets increase the activity of the synzymes. The structures of the 17 most active catalysts selectedfrom the library of complexes obtained with Cu2+ ion varied from 16 derivatives complexed withZn2+ ion. For all of them, a very high reaction rate during the preliminary phase of measurementswas followed by a substantial slowdown after 1 h. The catalytic activity gradually diminished aftersubsequent re-use. HPLC analysis of amide bond splitting confirmed that substrate consumptionproceeded in two stages. In the preliminary stage 24–40% of the substrate was rapidly hydrolysedfollowed by the substantially lower reaction rate. Nevertheless, using the most competentsynzymes product of hydrolysis was formed with a yield of 60–83% after 48h under mild andstrictly biomimetic conditions.

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“…Hydrolysis of esters or amides using natural chymotrypsin is usually carried out at room temperatures because of the denaturation of the enzyme at higher temperatures. The optimum temperature for catalytic amidolysis using MIPs was found to be 45-50 C [63][64][65][66][67].…”

Section: Effect Of Temperaturementioning

confidence: 99%

“…We extended the investigation with the organic analogues -4-vinylimidazole, allyl alcohol, methacrylic acid -of methacrylated amino acid monomers [65]. The achiral monomers formed pre-polymer complex with both L-and D-TSAs from the rac-TSA and fabricated cavities with both L-and D configuration in the polymer matrix.…”

Section: Transition State Analogue Imprinted Amidasesmentioning

confidence: 99%

“…The enzyme mimic polymer catalyst exhibited bell-shaped pH profile in catalytic amidolysis like natural chymotrypsin. The optimum rate was observed at pH 7.75. in acidic medium protonation of the imidazole moiety is thought to be the retarding force of catalytic rate [63][64][65][66][67]. However, MIPs possess many disadvantageous: it is hard to completely remove the print molecule from MIPs; the imprinted polymer is insoluble; and the polymer contains heterogeneous binding sites.…”

Section: Effect Of Phmentioning

confidence: 99%

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Design, synthesis and characterization of enzyme-analogue-built polymer catalysts as artificial hydrolases

Mathew

Thomas

Devaky

2019

Artificial Cells, Nanomedicine, and Biotechnology

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In this review, the concept and various strategies in molecular imprinting is discussed briefly. How the concept of transition state analogue can be used to design a template to prepare catalytic imprinted polymers is described in detail. The use of the "bait and switch" approach and alternative covalent template strategies show how functional groups which assist in the catalytic properties can be assembled within the imprint. Thus, there are so many reports on P catalyzed reactions. Owing to their advantageous properties over natural biological recognition agents, molecularly imprinted polymers (MIPs) therefore offer great potential for various applications.

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Amidase activity of phosphonate TSA-built polymer catalysts derived from organic monomers in the amidolysis of amino acid p-nitroanilides

Cited by 11 publications

References 32 publications

Synthetic Catalysts Inspired by Hydrolytic Enzymes

Synthetic Catalysts Inspired by Hydrolytic Enzymes

N-Lipidated Amino Acids and Peptides Immobilized on Cellulose Able to Split Amide Bonds

Design, synthesis and characterization of enzyme-analogue-built polymer catalysts as artificial hydrolases

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