A surfactant–heme–sulfonyl imidazole system as a nano-artificial enzyme

Kermani, Hanie Ahmadzade; Shockravi, Abbas; Moosavi-Movahedi, Zainab; Khalafi-Nezhad, Ali; Behrouz, Somayeh; Tsai, Fu-Yuan; Hakimelahi, G. H.; Seyedarabi, Arefeh; Moosavi‐Movahedi, Ali Akbar

doi:10.1007/s13738-013-0233-5

Cited by 12 publications

(1 citation statement)

References 4 publications

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“…The overall host–guest interactions of selective inhibitors such as 4,5‐diarylimidazoles consist of hydrogen bond formation and van der waals forces . These stereoelectronic interactions can be affected by electron‐withdrawing and electron‐donating groups . A common base structural motif of the most COX‐2 selective inhibitors consists of two aryl groups linked to adjoining atoms of a central ring, which can be homocyclic or heterocyclic .…”

Section: Introductionmentioning

confidence: 99%

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-¹⁴C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

Shirvani

Shockravi

Amini

et al. 2016

J. Label Compd. Radiopharm

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Section: Introductionmentioning

confidence: 99%

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-¹⁴C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

Shirvani

Shockravi

Amini

et al. 2016

J. Label Compd. Radiopharm

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A Cost‐Effective Hemin‐Based Artificial Enzyme Allows for Practical Applications

Qiu,

He,

Liu

et al. 2024

Advanced Science

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Nanomaterials excel in mimicking the structure and function of natural enzymes while being far more interesting in terms of structural stability, functional versatility, recyclability, and large‐scale preparation. Herein, the story assembles hemin, histidine analogs, and G‐quadruplex DNA in a catalytically competent supramolecular assembly referred to as assembly‐activated hemin enzyme (AA‐heminzyme). The catalytic properties of AA‐heminzyme are investigated both in silico (by molecular docking and quantum chemical calculations) and in vitro (notably through a systematic comparison with its natural counterpart horseradish peroxidase, HRP). It is found that this artificial system is not only as efficient as HRP to oxidize various substrates (with a turnover number kcat of 115 s−1) but also more practically convenient (displaying better thermal stability, recoverability, and editability) and more economically viable, with a catalytic cost amounting to <10% of that of HRP. The strategic interest of AA‐heminzyme is further demonstrated for both industrial wastewater remediation and biomarker detection (notably glutathione, for which the cost is decreased by 98% as compared to commercial kits).

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Synthesis and catalytic evaluation of Fe₃O₄/MWCNTs nanozyme as recyclable peroxidase mimetics: Biochemical and physicochemical characterization

Salarizadeh

Sadri

Sajedi

2017

Applied Organom Chemis

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In this research, the nanocomposite of multiwalled carbon nanotubes and magnetic metal oxide nanoparticles (Fe3O4/MWCNTs), as enzyme mimetic, was synthesized using an in situ chemical reduction method. The structure, composition and morphology of the prepared Fe3O4/MWCNT nanocomposite materials were characterized using X‐ray diffraction, FT‐IR and scanning electron microscopy with energy dispersive X‐ray spectroscopy, respectively. The magnetic properties of the nanocomposite were investigated by the vibrating sample magnetometer. A colorimetric system involving nanozyme, phenol/4‐aminoantipyrine and H2O2 was utilized for the determination of peroxidase mimetic catalytic assay. The obtained results confirmed that the synthesis of Fe3O4/MWCNTs nanostructures was successful. It was found that Fe3O4/MWCNTs nanohybrid exhibited peroxidase‐like activity without any pH limitation. Colorimetric data demonstrated that the prepared nanocatalyst had higher catalytic activity toward H2O2 than MWCNTs. The kinetic parameters of the nanozyme, Km and Vmax, were estimated to be 8.3 mm and 1.4 mm min−1, respectively. The Fe3O4/MWCNTs nanostructures were also successfully applied for glucose detection. In addition, peroxidase‐like activity of the nanozyme increased in the presence of butyl‐imidazolium bromide ionic liquid. These biomimetic catalysts have some advantages, such as simplicity, stability, reusability and cost effectiveness, which makes them great candidates to be used in various fields of biotechnology applications.

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A surfactant–heme–sulfonyl imidazole system as a nano-artificial enzyme

Cited by 12 publications

References 4 publications

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-¹⁴C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-¹⁴C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

A Cost‐Effective Hemin‐Based Artificial Enzyme Allows for Practical Applications

Synthesis and catalytic evaluation of Fe₃O₄/MWCNTs nanozyme as recyclable peroxidase mimetics: Biochemical and physicochemical characterization

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A surfactant–heme–sulfonyl imidazole system as a nano-artificial enzyme

Cited by 12 publications

References 4 publications

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-14C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-14C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

A Cost‐Effective Hemin‐Based Artificial Enzyme Allows for Practical Applications

Synthesis and catalytic evaluation of Fe3O4/MWCNTs nanozyme as recyclable peroxidase mimetics: Biochemical and physicochemical characterization

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Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-¹⁴C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

Synthesis of 2-(methylsulfonyl)-5-(4-(methylsulfonyl) phenyl)-4-phenyl-1H-[5-¹⁴C]imidazole, a selective COX-2 inhibitor, via asymmetrical benzoins

Synthesis and catalytic evaluation of Fe₃O₄/MWCNTs nanozyme as recyclable peroxidase mimetics: Biochemical and physicochemical characterization