Copper(II) Ions Originating from CuBTC MOF Act as a Soluble Catalyst in the Friedländer Synthesis DOI

Tessa Whitaker,

Robert R. Tuttle,

Jonathan E. Thai

et al.

ACS Applied Materials & Interfaces, Journal Year: 2024, Volume and Issue: 16(17), P. 22641 - 22647

Published: April 22, 2024

The copper-based metal-organic framework (MOF), CuBTC (where H3BTC = benzene-1,3,5-tricarboxylate), has been reported as a reusable heterogeneous catalyst for the Friedländer synthesis of substituted quinolines, which are desirable targets in pharmaceutical industry. Because this application, we further investigated CuBTC-catalyzed 3-acetyl-2-methyl-4-phenylquinoline. was synthesized in-house and used synthesis. Fresh were analyzed using scanning electron microscopy (SEM), powder X-ray diffraction (pXRD), photoelectron spectroscopy (XPS). shows structural breakdown pXRD patterns SEM images. Despite breakdown, desired product, 3-acetyl-2-methyl-4-phenylquinoline, is still produced moderate yield (76.3% ± 0.2), confirmed via time-of-flight mass spectrometry nuclear magnetic resonance spectroscopy. Inductively coupled plasma atomic emission recovered supernatant solution indicates presence copper(II) ions solution. Thus, hypothesized that standard conditions may degrade framework, resulting Control experiments with from Cu(NO3)2·3H2O catalyzes reaction yields (75.6% 0.1) equal to MOF. Overall, our findings suggest acts source, originating MOF responsible observed catalysis.

Language: Английский

Confining enzymes in porous organic frameworks: from synthetic strategy and characterization to healthcare applications DOI
Siming Huang, Guosheng Chen, Gangfeng Ouyang

et al.

Chemical Society Reviews, Journal Year: 2022, Volume and Issue: 51(15), P. 6824 - 6863

Published: Jan. 1, 2022

This review comprehensively presents the cutting-edge advances of enzyme confinement using different porous organic frameworks.

Language: Английский

Citations

193
Recent progress in host–guest metal–organic frameworks: Construction and emergent properties DOI

Xiao−Ting Liu,

Binbin Qian,

Da−Shuai Zhang

et al.

Coordination Chemistry Reviews, Journal Year: 2022, Volume and Issue: 476, P. 214921 - 214921

Published: Nov. 16, 2022

Language: Английский

Citations

79
Diffusion-programmed catalysis in nanoporous material DOI Creative Commons
Suvendu Panda, Tanmoy Maity, Susmita Sarkar

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: Feb. 3, 2025

Abstract In the realm of heterogeneous catalysis, diffusion reactants into catalytically active sites stands as a pivotal determinant influencing both turnover frequency and geometric selectivity in product formation. While accelerated can elevate reaction rates, it often entails compromise selectivity. Porous catalysts, including metal-organic covalent organic frameworks, confront formidable obstacles regulating reactant rates. Consequently, chemical functionality catalysts typically governs This study presents an approach harnessing length to achieve improved manipulation reactant-active site residence time at augment kinetics. Through deployment thin film composed porous framework catalyst, we illustrate how programming within cross-flow microfluidic catalytic reactor concurrently amplify (exceeding 1000-fold) enhance ( ~ 2-fold) relative conventional nano/microcrystals catalyst one-pot reactor. diffusion-programed strategy represents robust solution surmount constraints imposed by bulk marking advancement design catalyst-driven reactions.

Language: Английский

Citations

4
MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents DOI
Raphael Greifenstein, Tim Ballweg, Tawheed Hashem

et al.

Angewandte Chemie International Edition, Journal Year: 2022, Volume and Issue: 61(18)

Published: Feb. 8, 2022

Fully exploiting the potential of enzymes in cell-free biocatalysis requires stabilization catalytically active proteins and their integration into efficient reactor systems. Although recent years initial steps towards immobilization such biomolecules metal-organic frameworks (MOFs) have been taken, these demonstrations limited to batch experiments aqueous conditions. Here we demonstrate a MOF-based continuous flow enzyme system, with high productivity stability, which is also suitable for organic solvents. Under conditions, stability was increased 30-fold, space-time yield exceeded that obtained other strategies by an order magnitude. Importantly, infiltration MOF did not require additional functionalization, thus allowing time- cost-efficient fabrication biocatalysts using label-free enzymes.

Language: Английский

Citations

66
Boosting Protein Encapsulation through Lewis-Acid-Mediated Metal–Organic Framework Mineralization: Toward Effective Intracellular Delivery DOI Creative Commons
Jesús Cases Díaz, Beatriz Lozano‐Torres, Mónica Giménez‐Marqués

et al.

Chemistry of Materials, Journal Year: 2022, Volume and Issue: 34(17), P. 7817 - 7827

Published: Aug. 29, 2022

Encapsulation of biomolecules using metal-organic frameworks (MOFs) to form stable biocomposites has been demonstrated be a valuable strategy for their preservation and controlled release, which however restricted specific electrostatic surface conditions. We present Lewis-acid-mediated general in situ that promotes the spontaneous MOF growth on broad variety proteins, first time, regardless nature. demonstrate MOFs based cations exhibiting considerable inherent acidity such as MIL-100(Fe) enable efficient biomolecule encapsulation, including elusive alkaline proteins previously inaccessible by well-developed azolate-based encapsulation. Specifically, we prove scaffold encapsulation group very different isoelectric points (5 < pI 11), allowing triggered release under biocompatible conditions retaining activity after exposure denaturing environments. Finally, potential myoglobin-carrying biocomposite facilitate delivery O2 into hypoxic human lung carcinoma A549 cells, overcoming hypoxia-associated chemoresistance.

Language: Английский

Citations

50
Metal-organic frameworks for the adsorptive removal of pharmaceutically active compounds (PhACs): Comparison to activated carbon DOI
Nicholaus Prasetya, I Gede Wenten, Matthias Franzreb

et al.

Coordination Chemistry Reviews, Journal Year: 2022, Volume and Issue: 475, P. 214877 - 214877

Published: Oct. 15, 2022

Language: Английский

Citations

47
Hierarchical covalent organic framework-foam for multi-enzyme tandem catalysis DOI Creative Commons
Satyadip Paul, Mani Gupta, Kaushik Dey

et al.

Chemical Science, Journal Year: 2023, Volume and Issue: 14(24), P. 6643 - 6653

Published: Jan. 1, 2023

We have developed a covalent organic framework foam with ordered and disordered pores which can immobilize various enzymes towards one-pot tandem glucose synthesis from CMC excellent recyclability be used in biofuel production.

Language: Английский

Citations

33
Covalent Organic Frameworks for the Purification of Recombinant Enzymes and Heterogeneous Biocatalysis DOI
Satyadip Paul, Mani Gupta, Ashok Kumar Mahato

et al.

Journal of the American Chemical Society, Journal Year: 2023, Volume and Issue: 146(1), P. 858 - 867

Published: Dec. 30, 2023

Recombinant enzymes have gained prominence due to their diverse functionalities and specificity are often a greener alternative in biocatalysis. This context makes purifying recombinant from host cells other impurities crucial. The primary goal is isolate the pure enzyme of interest ensure its stability under ambient conditions. Covalent organic frameworks (COFs), renowned for well-ordered structure permeability, offer promising approach histidine-tagged (His-tagged) enzymes. Furthermore, immobilizing within COFs represents growing field heterogeneous In this study, we developed flow-based technology utilizing nickel-infused covalent framework (Ni-TpBpy COF) combine two distinct processes: purification His-tagged immobilization simultaneously. Our work primarily focuses on three β-glucosidase, cellobiohydrolase, endoglucanase as well proteins with varying molecular weights, namely, green fluorescent protein (27 kDa) BG Rho (88 kDa). We employed Ni-TpBpy column matrix showcase versatility our system. Additionally, successfully obtained COF immobilized enzymes, which can serve catalyst hydrolysis p-nitrophenyl-β-d-glucopyranoside carboxymethylcellulose. These demonstrated catalytic activity comparable that free counterparts, added advantages recyclability enhanced conditions an extended period, ranging 60 90 days. contrasts do not maintain effectively over time.

Language: Английский

Citations

31
Covalent Organic Framework Cladding on Peptide-Amphiphile-Based Biomimetic Catalysts DOI
Ashok Kumar Mahato, Sumit Pal, Kaushik Dey

et al.

Journal of the American Chemical Society, Journal Year: 2023, Volume and Issue: 145(23), P. 12793 - 12801

Published: June 2, 2023

Peptide-based biomimetic catalysts are promising materials for efficient catalytic activity in various biochemical transformations. However, their lack of operational stability and fragile nature non-aqueous media limit practical applications. In this study, we have developed a cladding technique to stabilize within porous covalent organic framework (COF) scaffolds. This methodology allows the homogeneous distribution peptide nanotubes inside COF (TpAzo TpDPP) backbone, creating strong noncovalent interactions that prevent leaching. We synthesized two different peptide-amphiphiles, C10FFVK C10FFVR, with lysine (K) arginine (R) at C-termini, respectively, which formed nanotubular morphologies. The peptide-amphiphile exhibit enzyme-like behavior efficiently catalyze C–C bond cleavage buffer medium (pH 7.5). produced structures TpAzo–C10FFVK TpDPP–C10FFVK through by using interfacial crystallization (IC). encased as well solvents (such acetonitrile, acetone, dichloromethane). catalyst, being heterogeneous, is easily recoverable, enabling reaction be performed multiple cycles. Additionally, synthesis thin films facilitates catalysis flow. As control, another peptide-amphiphile, also forms tubular assemblies. By depositing TpAzo crystallites on C10FFVR IC, TpAzo–C10FFVR expectedly did not show catalysis, suggesting critical role lysines TpAzo–C10FFVK.

Language: Английский

Citations

29
A Synergetic Pore Compartmentalization and Hydrophobization Strategy for Synchronously Boosting the Stability and Activity of Enzyme DOI

Lihong Guo,

Rongwei He,

Guosheng Chen

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(25), P. 17189 - 17200

Published: June 12, 2024

Spatial immobilization of fragile enzymes using a nanocarrier is an efficient means to design heterogeneous biocatalysts, presenting superior stability and recyclability pristine enzymes. An immobilized enzyme, however, usually compromises its catalytic activity because inevasible mass transfer issues the unfavorable conformation changes in confined environment. Here, we describe synergetic metal–organic framework pore-engineering strategy trap lipase (an important hydrolase), which confers lipase-boosted simultaneously. The hierarchically porous NU-1003, featuring interconnected mesopore micropore channels, precisely modified by chain-adjustable fatty acids on channel, into trapped. pore structure ensures communication between trapped exterior media, while acid-mediated hydrophobic can activate opening interfacial interaction. Such dual compartmentalization hydrophobization activation effects render center highly accessible, resulting 1.57-fold 2.46-fold activities as native ester hydrolysis enantioselective catalysis. In addition, feasibility these biocatalysts for kinetic resolution enantiomer also validated, showing much higher efficiency than lipase.

Language: Английский

Citations

14