The Experts below are selected from a list of 14025 Experts worldwide ranked by ideXlab platform
Jinsong Ren - One of the best experts on this subject based on the ideXlab platform.
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a series of mof ce based nanozymes with dual Enzyme like activity disrupting biofilms and hindering recolonization of bacteria
Biomaterials, 2019Co-Authors: Zhengwei Liu, Faming Wang, Jinsong RenAbstract:Notorious bacterial biofilms are becoming severe threats to public health worldwide. As the important component in biofilm extracellular polymeric substances (EPS), extracellular DNA (eDNA) has been manifested to connect different EPS components and bacteria together, leading biofilms hard to eliminate. Herein a series of MOF/Ce-based nanozymes with deoxyribonuclease (DNase) and peroxidase mimetic activities have been designed and synthesized for combating biofilms. The cerium (IV) complexes (DNase mimics) are capable of hydrolyzing eDNA and disrupting established biofilms, while the MOF with peroxidase-like activity can kill bacteria exposed in dispersed biofilms in the presence of H2O2. This can avoid the recolonization of bacteria and recurrence of biofilms. Given the fact that single-modal antibacterial agent is difficult to drastically eradicate biofilms, the marriage of two kinds of nanozymes is a rational strategy to acquire enhanced performance in combating biofilms. Besides, the utilization of nanozymes circumvents drawbacks of natural Enzymes which are costly and vulnerable. Further studies have demonstrated that this kind of Artificial Enzyme with dual Enzyme-mimetic activities can penetrate the biofilms, and inhibit bacterial biofilm formation intensively. Consistently, in vivo anti-biofilm application in treating subcutaneous abscess exhibits commendable wound healing and admirable bactericidal effect. To the best of our knowledge, it is the first time to devise an integrated nanozyme based on the peroxidase-like activity of MOF to eliminate biofilms and kill bacteria on site. This work may promote the application of MOF in the antibacterial field.
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Enzyme Mimicry for Combating Bacteria and Biofilms
2018Co-Authors: Zhaowei Chen, Zhenzhen Wang, Jinsong RenAbstract:ConspectusBacterial infection continues to be a growing global health problem with the most widely accepted treatment paradigms restricted to antibiotics. However, antibiotics overuse and misuse have triggered increased multidrug resistance, frustrating the therapeutic outcomes and leading to higher mortalities. Even worse, the tendency of bacteria to form biofilms on living and nonliving surfaces further increases the difficulty in confronting bacteria because the extracellular matrix can act as a robust barrier to prevent the penetration of antibiotics and resist environmental stress. As a result, the inability to completely eliminate bacteria and biofilms often leads to persistent infection, implant failure, and device damage. Therefore, it is of paramount importance to develop alternative antimicrobial agents while avoiding the generation of bacterial resistance. Taking lessons from natural Enzymes for destroying cellular structural integrity or interfering with metabolisms such as proliferation, quorum sensing, and programmed death, the construction of Artificial Enzymes to mimic the Enzyme functions will provide unprecedented opportunities for combating bacteria. Moreover, compared to natural Enzymes, Artificial Enzymes possess much higher stability against stringent conditions, easier tunable catalytic activity, and large-scale production for practical use.In this Account, we will focus on our recent progress in the design and synthesis of Artificial Enzymes as a new generation of “antibiotics”, which have been demonstrated as promising applications in planktonic bacteria inactivation, wound/lung disinfection, as well as biofilm inhibition and dispersion. First, we will introduce direct utilization of the intrinsic catalytic activities of Artificial Enzymes without dangerous chemical auxiliaries for killing bacteria under mild conditions. Second, to avoid the toxicity caused by overdose of H2O2 in conventional disinfections, we leveraged Artificial Enzymes with peroxidase-mimic activities to catalyze the generation of hydroxyl radicals at low H2O2 levels while achieving efficient antibacterial outcomes. Importantly, the feasibility of these Artificial Enzymes was further demonstrated in vivo by mitigating mice wound and lung disinfection. Third, by combining Artificial Enzymes with stimuli-responsive materials, smart on-demand therapeutic modalities were constructed for thwarting bacteria in a controllable manner. For instance, a photoswitchable “Band-Aid”-like hydrogel doped with Artificial Enzymes was developed for efficiently killing bacteria without compromising mammal cell proliferation, which was promising for accelerating wound healing. Lastly, regarding the key roles that extracellular DNAs (eDNAs) play in maintaining biofilm integrity, we further designed a multinuclear metal complex-based DNase-mimetic Artificial Enzyme toward cleaving the eDNA for inhibiting biofilm formation and dispersing the established biofilms. We expect that our rational designs would boost the development of Artificial Enzymes with different formulations as novel antibacterial agents for clinical and industrial applications
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design of surface active Artificial Enzyme particles to stabilize pickering emulsions for high performance biphasic biocatalysis
Advanced Materials, 2016Co-Authors: Zhaowei Chen, Jinsong Ren, Chuanqi Zhao, Bernard P BinksAbstract:Surface-active Artificial Enzymes (SAEs) are designed and constructed by a general and novel strategy. These SAEs can simultaneously stabilize Pickering emulsions and catalyze biphasic biotransformation with superior enzymatic stability and good re-usability; for example, for the interfacial conversion of hydrophobic p-nitrophenyl butyrate into yellow water-soluble p-nitrophenolate catalyzed by esterase-mimic SAE.
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nanocomposite incorporating v2o5 nanowires and gold nanoparticles for mimicking an Enzyme cascade reaction and its application in the detection of biomolecules
Chemistry: A European Journal, 2014Co-Authors: Peng Shi, Jinsong RenAbstract:Artificial Enzyme mimics are a current research interest, and many nanomaterials have been found to display Enzyme-mimicking activity. However, to the best of our knowledge, there have not hitherto been any reports on the use of pure nanomaterials to construct a system capable of mimicking an Enzyme cascade reaction. Herein, we describe the construction of a novel nanocomposite consisting of V2O5 nanowires and gold nanoparticles (AuNPs) through a simple and facile chemical method, in which V2O5 and AuNPs possess intrinsic peroxidase and glucose oxidase (GOx)-like activity, respectively. Results suggest that this material can mimic the Enzyme cascade reaction of horseradish peroxidase (HRP) and GOx. Based on this mechanism, a direct and selective colorimetric method for the detection of glucose has been successfully designed. Because single-strand and double-strand DNA (ssDNA and dsDNA) have different deactivating effects on the GOx-like activity of AuNPs, the sensing of target complementary DNA can also be realized and disease-associated single-nucleotide polymorphism of DNA can be easily distinguished. Our study opens a new avenue for the use of nanomaterials in Enzyme mimetics, and holds promise for the further exploration of nanomaterials in creating alternative catalytic systems to natural Enzymes.
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Artificial evolution of graphene oxide chemzyme with enantioselectivity and near infrared photothermal effect for cascade biocatalysis reactions
Small, 2014Co-Authors: Chuanqi Zhao, Jinsong RenAbstract:It is highly desirable and challenging when the chemzyme can be not only simply duplicating and imitating the properties of natural Enzymes, but also introducing additional new features for practical applications. Herein, we report a zinc-finger-protein like -helical chiral metallo-supramolecular complex ([Fe2L3](4+)) functionalized graphene oxide (GO-COOH) as a peroxidase mimic. This Artificial Enzyme integrates the characteristics of both chiral metallo-supramolecular complex and GO-COOH, and shows excellent catalytic activity.
Guoyue Shi - One of the best experts on this subject based on the ideXlab platform.
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colorimetric detection of carcinogenic aromatic amine using layer by layer graphene oxide cytochrome c composite
ACS Applied Materials & Interfaces, 2018Co-Authors: Min Zhang, Guoyue ShiAbstract:Graphene and its derivatives were found to be efficient modulators of Enzymes in various systems. However, the modulating mechanism was not well discussed for long time. Inspired by the Artificial Enzyme-enhancing property of graphene oxide (GO) toward cytochrome c (cyt. c), we have successfully fabricated a protein/GO hybrid structure via a layer-by-layer (LbL) strategy. The obtained LbL assemblies showed great enhancement in peroxidase activity of cyt. c, as well as excellent stability, resistance to extreme environment change, and also possibility for recycling by simple centrifugation without any obvious activity loss. The LbL cyt. c/GO hybrids were expanded to a colorimetric sensing system for the detection of carcinogenic aromatic amines. The probe showed high sensitivity and selectivity for aromatic amines over various competing soluble aromatic compounds and could be determined by the naked eye or portable devices. The working mechanism was well studied through kinetic evaluation, experimental characterization, and molecular dynamics simulations. This work does not only introduce a new graphene/protein hybrid material or a rapid and sensitive visualization of carcinogenic aromatic amines, but also spread the practical application of biomolecule-graphene interface strategy and further give a better understanding of the interaction of graphene and protein.
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Colorimetric Detection of Carcinogenic Aromatic Amine Using Layer-by-Layer Graphene Oxide/Cytochrome c Composite
2018Co-Authors: Min Zhang, Guoyue ShiAbstract:Graphene and its derivatives were found to be efficient modulators of Enzymes in various systems. However, the modulating mechanism was not well discussed for long time. Inspired by the Artificial Enzyme-enhancing property of graphene oxide (GO) toward cytochrome c (cyt. c), we have successfully fabricated a protein/GO hybrid structure via a layer-by-layer (LbL) strategy. The obtained LbL assemblies showed great enhancement in peroxidase activity of cyt. c, as well as excellent stability, resistance to extreme environment change, and also possibility for recycling by simple centrifugation without any obvious activity loss. The LbL cyt. c/GO hybrids were expanded to a colorimetric sensing system for the detection of carcinogenic aromatic amines. The probe showed high sensitivity and selectivity for aromatic amines over various competing soluble aromatic compounds and could be determined by the naked eye or portable devices. The working mechanism was well studied through kinetic evaluation, experimental characterization, and molecular dynamics simulations. This work does not only introduce a new graphene/protein hybrid material or a rapid and sensitive visualization of carcinogenic aromatic amines, but also spread the practical application of biomolecule–graphene interface strategy and further give a better understanding of the interaction of graphene and protein
Huzhi Zheng - One of the best experts on this subject based on the ideXlab platform.
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enhancing the peroxidase like activity of ficin via heme binding and colorimetric detection for uric acid
Talanta, 2018Co-Authors: Yufang Yang, Yijuan Long, Yanjiao Pang, Huzhi ZhengAbstract:Abstract Ficin, a classical sulfhydryl protease, was found to possess intrinsic peroxidase-like activity. In this paper, we have put forward a novel strategy to improving the peroxidase-like activity of ficin through binding heme. Heme-ficin complexes were successfully obtained by simple one-step syntheticism. The results demonstrated that the catalytic activity and efficiency of heme-ficin complexes were about 1.7 times and 3 times higher than those of native ficin, respectively. Taking advantages of the high peroxidase-like activity, the heme-ficin complexes were used for colorimetric determination of uric acid with a low detection limit of 0.25 μM. Based on the excellent selectivity and sensitivity, we detected the concentration of uric acid in human serum successfully. On the basis of these findings, the heme-ficin complexes are promising for wide applications in various fields. Thus we not only optimized the peroxidase-like activity of the ficin, but also established a new strategy for development of Artificial Enzyme mimics by mimicking the architecture of the active site in horseradish peroxidase.
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fluorescein as an Artificial Enzyme to mimic peroxidase
Chemical Communications, 2016Co-Authors: Yufang Yang, Yijuan Long, Menglu Li, Yuming Huang, Huzhi ZhengAbstract:Fluorescein was found to possess intrinsic peroxidase-like activity, which could catalyze the oxidation of 3,3′,5,5′-tetramethylbenzidine (TMB) by H2O2 to produce a color reaction. It opens the possibility of using such small molecules as peroxidase-like catalysts.
Mengfan Wang - One of the best experts on this subject based on the ideXlab platform.
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constructing peptide based Artificial hydrolases with customized selectivity
Journal of Materials Chemistry B, 2019Co-Authors: Mingjie Zhu, Mengfan WangAbstract:Peptide-based materials are promising building blocks for the fabrication of Artificial Enzymes due to their proteic nature and tailorable structure. However, it is still a big challenge to create Artificial Enzymes with designable selectivity. In this study, the molecular imprinting strategy was combined with the self-assembly of Fmoc-FFH to create an Artificial hydrolase with specific selectivity. By using p-NPA as the imprinting template, we found that the imprinted polymer that was coated on the surface of the catalytic peptide nanofibers provided a specific binding site to p-NPA, hence enhancing the catalytic efficiency of the Artificial hydrolase. Furthermore, we confirmed that the substrate selectivity of this Artificial Enzyme can be customized by changing the imprinting template. The obtained catalyst is recyclable and exhibits a higher catalytic activity at a wider reaction temperature and pH due to the introduction of the polymer. This study provides a new approach to constructing Enzyme mimics with customized substrate selectivity based on the peptide-based material platform.
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enhancing the activity of peptide based Artificial hydrolase with catalytic ser his asp triad and molecular imprinting
ACS Applied Materials & Interfaces, 2016Co-Authors: Mengfan Wang, Xiaojing LiuAbstract:In this study, an Artificial hydrolase was developed by combining the catalytic Ser/His/Asp triad with N-fluorenylmethoxycarbonyl diphenylalanine (Fmoc-FF), followed by coassembly of the peptides into nanofibers (CoA-HSD). The peptide-based nanofibers provide an ideal supramolecular framework to support the functional groups. Compared with the self-assembled catalytic nanofibers (SA-H), which contain only the catalytic histidine residue, the highest activity of CoA-HSD occurs when histidine, serine, and aspartate residues are at a ratio of 40:1:1. This indicates that the well-ordered nanofiber structure and the synergistic effects of serine and aspartate residues contribute to the enhancement in activity. Additionally, for the first time, molecular imprinting was applied to further enhance the activity of the peptide-based Artificial Enzyme (CoA-HSD). p-NPA was used as the molecular template to arrange the catalytic Ser/His/Asp triad residues in the proper orientation. As a result, the activity of imprint...
Xiaogang Qu - One of the best experts on this subject based on the ideXlab platform.
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Nanozymes: Classification, Catalytic Mechanisms, Activity Regulation, and Applications
Chemical Reviews, 2019Co-Authors: Yanyan Huang, Xiaogang QuAbstract:Because of the high catalytic activities and substrate specificity, natural Enzymes have been widely used in industrial, medical, and biological fields, etc. Although promising, they often suffer from intrinsic shortcomings such as high cost, low operational stability, and difficulties of recycling. To overcome these shortcomings, researchers have been devoted to the exploration of Artificial Enzyme mimics for a long time. Since the discovery of ferromagnetic nanoparticles with intrinsic horseradish peroxidase-like activity in 2007, a large amount of studies on nanozymes have been constantly emerging in the next decade. Nanozymes are one kind of nanomaterials with enzymatic catalytic properties. Compared with natural Enzymes, nanozymes have the advantages such as low cost, high stability and durability, which have been widely used in industrial, medical, and biological fields. A thorough understanding of the possible catalytic mechanisms will contribute to the development of novel and high-efficient nanozymes, and the rational regulations of the activities of nanozymes are of great significance. In this review, we systematically introduce the classification, catalytic mechanism, activity regulation as well as recent research progress of nanozymes in the field of biosensing, environmental protection, and disease treatments, etc. in the past years. We also propose the current challenges of nanozymes as well as their future research focus. We anticipate this review may be of significance for the field to understand the properties of nanozymes and the development of novel nanomaterials with Enzyme mimicking activities.
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mesoporous encapsulated chiral nanogold for use in enantioselective reactions
Angewandte Chemie, 2018Co-Authors: Hongcheng Xu, Ya Zhou, Silvina Matysiak, Xiaogang QuAbstract:: Although various nanomaterials have been designed for biocatalysis, few of them can accelerate chemical reactions with high selectivity and stereocontrol, which remains them from being perfect alternatives to nature Enzymes. Herein, inspired by the natural Enzymes, an enantioselective nanomaterial has been constructed, with gold nanoparticles (AuNPs) as active centers, chiral cysteine (Cys) as selectors for chiral recognition, and expanded mesoporous silica (EMSN) as a skeleton of the Artificial Enzyme. In the oxidation of chiral 3,4-dihydroxy-phenylalanine (DOPA), the nanozyme with d-Cys shows preference to l-DOPA while the Artificial Enzyme with l-Cys shows preference to d-DOPA. Subsequent calculation of apparent steady-state kinetic parameters and activation energies together with molecular dynamics (MD) simulations showed that the different affinity precipitated by hydrogen bonding formation between chiral Cys and DOPA is the origin of chiral selectivity.
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Artificial Enzyme based logic operations to mimic an intracellular Enzyme participated redox balance system
Chemistry: A European Journal, 2017Co-Authors: Yanyan Huang, Fang Pu, Xiaogang QuAbstract:Owing to the biocatalytic properties of Artificial Enzymes and the redox characteristic of glutathione, a colorimetric and resettable biological operation was successfully designed to mimic Enzyme-participated redox balance in living systems. As one promising candidate of a natural Enzyme, Artificial Enzyme possesses many advantages and has been used in numerous fields. Similar to natural Enzymes, communications are also present between different Artificial Enzymes. With the assistance of four Artificial Enzymes, three simple biological logic gates were fabricated to help us deepen the understanding of communications between Artificial Enzymes. In the presence of glutathione, the system could be easily reset without any complicated procedures. We prospect that this work may push forward the exploration of communications between different Artificial Enzymes and the design of novel Artificial Enzyme-based biological gates or nanodevices. We hope that our mimic system may help us further understand the functioning of complex biological pathways in biological systems.
