Oxidase-Mimetic Nanocatalyst Based on Geometry-Dependent Biomolecular Self-Assembly

Li, Shan; Wu, Haifeng; Liu, Yuanxi; Zhang, Baoli; Xu, Shichao; Wang, Zhen-Gang

doi:10.1021/acs.chemmater.3c02028

Cited by 3 publications

(3 citation statements)

References 49 publications

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“…Additionally, replacing GMP with flavin adenine dinucleotide (FAD) composed of a flavin ring and adenine can result in the specific association of the flavin moiety to fluorenyl rings, facilitating the close proximity of the amino acid and adenine and thus creating a heterogeneous ligand environment (Figure c(i)). Fmoc-Lys/FAD/Cu 2+ has a 10-fold and 2.2-fold higher efficiency than Fmoc-Lys/AMP/Cu 2+ and Fmoc-Lys/GMP/Cu 2+ , respectively, despite stronger affinity of guanine to Cu 2+ than adenine (Figure c(ii)).…”

Section: Distribute the Ligand Groups For Metal-dependent Catalytic S...mentioning

confidence: 99%

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Self-Assembly of Multimolecular Components for Engineering Enzyme-Mimetic Materials

Xu,

Liu,

Zhang

et al. 2024

Acc. Mater. Res.

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Metrics & MoreArticle Recommendations CONSPECTUS: Natural enzymes, with their intricate three-dimensional structures, facilitate a wide array of biochemical reactions with exceptional precision and speed. The catalytic capabilities of enzymes arise from the distinctive structures of their active sites, where functional groups collaborate or aid cofactors (organic or ionic) in binding substrates with specificity and catalyzing transformations. Inspired by the structure−function relationship of enzymes, supramolecular self-assembly, a bottom-up approach in nanofabrication, has been employed to create enzyme-mimetic catalysts. However, accurately replicating enzymatic active sites poses a formidable challenge, primarily because of the intricacies in mimicking the complexity of natural protein folding. Many natural biological systems, such as tryptophan synthase or ribosomes, rely on the association of multiple component subunits, each maintaining its structural integrity, to enable efficient and versatile functionalities. The hierarchical self-assembly principles observed in these systems have inspired us to design and self-assemble complementary molecular building blocks that form individual folding or aggregating structures, allowing for precise control over the distribution of reactive groups to create enzyme-like active sites. The customization of either component without disrupting folding structures enables the flexible engineering of catalytic properties. This Account will primarily focus on employing the self-assembly of multiple molecular components, drawing from research progress in our lab, to construct enzyme-mimetic catalysts with built-in metal-dependent or metal-free active sites. The structure−function relationship of these catalysts will be highlighted.To fabricate metal-dependent enzymatic sites, such as heme pockets or copper sites, within the synthetic materials, we create a supramolecular scaffold for stabilizing hemin or forming a copper cluster, followed by the introduction of a second component to enhance substrate adsorption or metal reactivity. The resulting enzyme mimics exhibit remarkable synergistic catalytic activities and possess great stability against the harsh conditions, such as high temperatures, high ionic strength, and cyclic acidification/ neutralization treatment. They can be engineered to possess tailorable selectivity toward specific chirality or sizes of substrates and can be externally stimulated to switch between ON/OFF states. These mimics have shown great performances in the sensing of biomolecules of interest, biomass degradation, and aiding in the understanding of the catalytic mechanism of native enzymes. To achieve metal-free catalysis, we introduce a "driving" component to the catalytic component to guide the formation of the assemblies mimicking the activity of hydrolases, photodecarboxylase, or photo-oxidase, with applications in peptide modifications or antibacterial therapy. Moreover, organized components like histidine can catalyze the reactions achieved by he...

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Section: Distribute the Ligand Groups For Metal-dependent Catalytic S...mentioning

confidence: 99%

Section: Distribute the Ligand Groups For Metal-dependent Catalytic S...mentioning

confidence: 99%

Self-Assembly of Multimolecular Components for Engineering Enzyme-Mimetic Materials

Xu,

Liu,

Zhang

et al. 2024

Acc. Mater. Res.

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“…Artificial enzymes (AEs) are a flourishing new class of bionic materials with similar biological activities to natural products but are more durable and adjustable than their natural counterparts. They have been widely employed in the application of biosensors, biosynthesis, biotherapeutics, etc. − Particularly, oxidase-like AEs show extensive promise for treating bacterial infections and tumors, due to their efficient catalytic ability to produce toxic reactive oxygen species (ROS). − Despite the great development, most oxidase-like AEs rely on hydrogen peroxide (H 2 O 2 ) in local pathological environments, and the catalytic performance still needs to be enhanced theoretically. A broad array of approaches have been proposed to modulate the electron structures and electron transfer (ET) process of active centers, the fundament of redox activities of AEs. − Since the local environments around active centers are pivotal for the reaction mechanism, the regulation of them by altering ligands and heteroatom is an effective way. , For instance, Li et al utilized transition-metal carbides to load atomic metal catalysts and achieved a boosted oxygen evolution reaction, due to effective ET originating from electronic interactions between metal atoms and carbide substrates .…”

Section: Introductionmentioning

confidence: 99%

Generating Reactive Oxygen Species by a Dual-Catalytic Metal–organic Framework-based Nanozyme against Drug-resistant Bacteria Infection

Ding,

Meng,

Song

et al. 2024

Chem. Mater.

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Oxidase-like artificial enzymes (AEs) are rapidly developing for their attractive reactive oxygen species (ROS)generating capacity in biological applications. However, efficient strategies to improve the AE catalytic performance by modulating the electron transfer (ET) process remain limited. Herein, a new electron transfer pathway in the de novo-designed MOF-based oxidase mimics (ZCA-X) is reported. The electron structure of the active center is regulated to form a unique Au−N−Cu domain for boosting ROS against drug-resistant bacteria. Unlike classical cascade catalytic systems depending on hydrogen peroxide or photocatalysts with complex regulation of band structure, the oxidase-like ZCA-20 catalyzes oxygen reduction via a direct four-ET process without simulation or a specific substrate. The Au−N−Cu active domain formed by charge transfer between Au NCs and CuN 4 single site exhibits high catalytic efficiency (k cat = 3.61 s −1 ), generating ROS as intermediate products. ZCA-20 AE is employed in catalytic eradication against drug-resistant bacteria in ROS-mediated structural damage, showing remarkable therapeutic effects both in vitro and in vivo. This strategy of modulating the ET process by coupling different active sites might inspire the development of new AEs with high selectivity and enzymatic activity.

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Peptide nanozymes: An emerging direction for functional enzyme mimics

He,

Ma,

Zheng

et al. 2024

Bioactive Materials

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Oxidase-Mimetic Nanocatalyst Based on Geometry-Dependent Biomolecular Self-Assembly

Cited by 3 publications

References 49 publications

Self-Assembly of Multimolecular Components for Engineering Enzyme-Mimetic Materials

Self-Assembly of Multimolecular Components for Engineering Enzyme-Mimetic Materials

Generating Reactive Oxygen Species by a Dual-Catalytic Metal–organic Framework-based Nanozyme against Drug-resistant Bacteria Infection

Peptide nanozymes: An emerging direction for functional enzyme mimics

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