A Photochemoenzymatic Hunsdiecker‐Borodin‐Type Halodecarboxylation of Ferulic Acid

Zippilli, Claudio; Bartolome, Miguel Jimenez; Hilberath, Thomas; Botta, Lorenzo; Hollmann, Frank; Saladino, Raffaele

doi:10.1002/cbic.202200367

Cited by 6 publications

(4 citation statements)

References 23 publications

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“…45 CiVCPO was purified via heat treatment according to a recently reported protocol. 46 Preparation of rAaeUPO. The expression-engineered variant of the recombinant unspecific peroxygenase from A. aegerita (rAaeUPO, PaDaI mutant) was used as a concentrated supernatant derived from a 2500 L pilot-scale cultivation of recombinant Pichia pastoris X-33.…”

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confidence: 99%

Enhancing the ROS Sensitivity of a Responsive Supramolecular Hydrogel Using Peroxizyme Catalysis

et al. 2023

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Hydrogels that can disintegrate upon exposure to reactive oxygen species (ROS) have the potential for targeted drug delivery to tumor cells. In this study, we developed a diphenylalanine (FF) derivative with a thioether phenyl moiety attached to the N-terminus that can form supramolecular hydrogels at neutral and mildly acidic pH. The thioether can be oxidized by ROS to the corresponding sulfoxide, which makes the gelator hydrolytically labile. The resulting oxidation and hydrolysis products alter the polarity of the gelator, leading to disassembly of the gel fibers. To enhance ROS sensitivity, we incorporated peroxizymes in the gels, namely, chloroperoxidase CiVCPO and the unspecific peroxygenase rAaeUPO. Both enzymes accelerated the oxidation process, enabling the hydrogels to collapse with 10 times lower H2O2 concentrations than those required for enzyme-free hydrogel collapse. These ROS-responsive hydrogels could pave the way toward optimized platforms for targeted drug delivery in the tumor microenvironment.

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Section: ■ Introductionmentioning

confidence: 99%

Enhancing the ROS Sensitivity of a Responsive Supramolecular Hydrogel Using Peroxizyme Catalysis

et al. 2023

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“…The organic hydroperoxide was able to activate HRP in the oxidation of substituted coumarins to yield bioactive homo‐ and heterodimers as an alternative to iodine‐based reagents (Figure 1; Panel A, pathway 1) [17–19] . A similar procedure was applied in the blue‐LED driven photo‐chemo‐enzymatic Hunsdiecker‐Borodin halo‐decarboxylation of aromatic carboxylic acids with chloro‐peroxidase, [20] as well as in the HRP‐pheomelanin UVA‐catalyzed oxidative coupling of substituted phenols [2] . The rigid tricyclic scaffold of Pummerer's ketones is a common pharmacophoric motif found in the morphine family of narcotic analgesics, such as in codeine, and in drugs active against Alzheimer's disease such as galanthamine and usnic acid [21] .…”

Section: Introductionmentioning

confidence: 99%

Blue‐LED Synthesis of Pummerer's Ketones by Peroxidase‐Lignin‐Catalyzed Oxidative Coupling of Substituted Phenols

Piccinino,

Ceccotti Vlas,

Gabellone

et al. 2023

Eur J Org Chem

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Pummerer's ketones resembling the tricyclic scaffold of bioactive natural substances were synthesized by blue‐LED driven Horseradish Peroxidase oxidative coupling of substituted phenols in 2‐methyltetrahydrofuran by using meso‐tetraphenylporphyrin as photosensitizer and dioxygen as primary oxidant. The application of functionalized lignin nanoparticles as a renewable and efficient platform for the immobilization of the enzyme extended the effectiveness of the overall process to heterogeneous catalysis under buffer limiting conditions.

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“…However, documented difficulties in the recombinant expression of Cf CPO and its sensitivity to excess hydrogen peroxide (H 2 O 2 ) loadings discouraged its use . Alternatively, we turned to the vanadium chloroperoxidase from Curvularia inaequalis ( Ci VCPO) due to its emergence as a robust biocatalyst for a number of synthetic transformations and superior versatility in toleration of high concentrations of H 2 O 2 and organic solvents . While this enzyme was recently explored as an effective catalyst for the chemoenzymatic decarboxylative halogenation of cinnamic acids, , its ability to perform this reaction on aromatic substrates has yet to be reported.…”

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Decarboxylative Bromooxidation of Indoles by a Vanadium Haloperoxidase

et al. 2023

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Halooxindoles are versatile building blocks for the construction of complex oxindole-containing targets of biological importance. Despite their synthetic value, catalytic methods to make 3-halooxindoles from readily available starting materials have remained undisclosed. We recently discovered that the chloroperoxidase from Curvularia inaequalis (CiVCPO) is a viable catalyst for the decarboxylative bromooxidation of 3-carboxyindoles to furnish 3-bromooxindoles with excellent regio-and chemoselectivity. In addition to the development of the synthetic method, this study provides evidence of a bromide recycling mechanism for the indole oxidation event. A discussion of the reaction development, substrate scope, mechanistic insights, and reaction applicability will be discussed herein.

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A Photochemoenzymatic Hunsdiecker‐Borodin‐Type Halodecarboxylation of Ferulic Acid

Cited by 6 publications

References 23 publications

Enhancing the ROS Sensitivity of a Responsive Supramolecular Hydrogel Using Peroxizyme Catalysis

Enhancing the ROS Sensitivity of a Responsive Supramolecular Hydrogel Using Peroxizyme Catalysis

Blue‐LED Synthesis of Pummerer's Ketones by Peroxidase‐Lignin‐Catalyzed Oxidative Coupling of Substituted Phenols

Decarboxylative Bromooxidation of Indoles by a Vanadium Haloperoxidase

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