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Advanced Drug Delivery Reviews Jun 2022Significant progress has been made in developing two-dimensional (2D) nanomaterials owing to their ultra-thin structure, high specific surface area, and many other... (Review)
Review
Significant progress has been made in developing two-dimensional (2D) nanomaterials owing to their ultra-thin structure, high specific surface area, and many other advantages. Recently, 2D nanomaterials with enzyme-like properties, especially peroxidase (POD)-like activity, are highly desirable for many biomedical applications. In this review, we first classify the types of 2D POD-like nanomaterials and then summarize various strategies for endowing 2D nanomaterials with POD-like properties. Representative examples of biomedical applications are reviewed, emphasizing in antibacterial, biosensing, and cancer therapy. Last, the future challenges and prospects of 2D POD-like nanomaterials are discussed. This review is expected to provide an in-depth understanding of 2D POD-like materials for biomedical applications.
Topics: Humans; Nanostructures; Peroxidase; Peroxidases
PubMed: 35398244
DOI: 10.1016/j.addr.2022.114269 -
European Journal of Heart Failure Sep 2023Mitiperstat (formerly AZD4831) is a novel selective myeloperoxidase inhibitor. Currently, no effective therapies target comorbidity-induced systemic inflammation, which... (Randomized Controlled Trial)
Randomized Controlled Trial
Rationale and design of ENDEAVOR: A sequential phase 2b-3 randomized clinical trial to evaluate the effect of myeloperoxidase inhibition on symptoms and exercise capacity in heart failure with preserved or mildly reduced ejection fraction.
AIMS
Mitiperstat (formerly AZD4831) is a novel selective myeloperoxidase inhibitor. Currently, no effective therapies target comorbidity-induced systemic inflammation, which may be a key mechanism underlying heart failure with preserved or mildly reduced ejection fraction (HFpEF/HFmrEF). Circulating neutrophils secrete myeloperoxidase, causing oxidative stress, microvascular endothelial dysfunction, interstitial fibrosis, cardiomyocyte remodelling and diastolic dysfunction. Mitiperstat may therefore improve function of the heart and other organs, and ameliorate heart failure symptoms and exercise intolerance. ENDEAVOR is a combined, seamless phase 2b-3 study of the efficacy and safety of mitiperstat in patients with HFpEF/HFmrEF.
METHODS
In phase 2b, approximately 660 patients with heart failure and ejection fraction >40% are being randomized 1:1:1 to mitiperstat 2.5 mg, 5 mg or placebo for 48 weeks. Eligible patients have baseline 6-min walk distance (6MWD) of 30-400 m with a <50 m difference between screening and randomization and Kansas City Cardiomyopathy Questionnaire total symptom score (KCCQ-TSS) ≤90 points at screening and randomization. The dual primary endpoints are change from baseline to week 16 in 6MWD and KCCQ-TSS. The sample size provides 85% power to detect placebo-adjusted improvements of 21 m in 6MWD and 6.0 points in KCCQ-TSS at overall two-sided alpha of 0.05. Safety is monitored throughout treatment, with a focus on maculopapular rash. In phase 3 of ENDEAVOR, approximately 820 patients will be randomized 1:1 to mitiperstat or placebo.
CONCLUSION
ENDEAVOR is the first phase 2b-3 study to evaluate whether myeloperoxidase inhibition can improve symptoms and exercise capacity in patients with HFpEF/HFmrEF.
Topics: Humans; Heart Failure; Stroke Volume; Exercise Tolerance; Peroxidase; Comorbidity; Heart Diseases
PubMed: 37470101
DOI: 10.1002/ejhf.2977 -
ACS Applied Bio Materials Feb 2024In biosensor development, silk fibroin is advantageous for providing transparent, flexible, chemically/mechanically stable, biocompatible, and sustainable substrates,...
In biosensor development, silk fibroin is advantageous for providing transparent, flexible, chemically/mechanically stable, biocompatible, and sustainable substrates, where the biorecognition element remains functional for long time periods. These properties are employed here in the production of point-of-care biosensors for resource-limited regions, which are able to display glucose levels without the need for external instrumentation. These biosensors are produced by photopatterning silk films doped with the enzymes glucose oxidase and peroxidase and photoelectrochromic molecules from the dithienylethene family acting as colorimetric mediators of the enzymatic reaction. The photopatterning results from the photoisomerization of dithienylethene molecules in the silk film from its initial uncolored opened form to its pink closed one. The photoisomerization is dose-dependent, and colored patterns with increasing color intensities are obtained by increasing either the irradiation time or the light intensity. In the presence of glucose, the enzymatic cascade reaction is activated, and peroxidase selectively returns closed dithienylethene molecules to their initial uncolored state. Color disappearance in the silk film is proportional to glucose concentration and used to distinguish between hypoglycemic (below 4 mM), normoglycemic (4-6 mM), and hyperglycemic levels (above 6 mM) by visual inspection. After the measurement, the biosensor can be regenerated by irradiation with UV light, enabling up to five measurement cycles. The coupling of peroxidase activity to other oxidoreductases opens the possibility to produce long-life reusable smart biosensors for other analytes such as lactate, cholesterol, or ethanol.
Topics: Silk; Colorimetry; Peroxidases; Biosensing Techniques; Peroxidase; Glucose
PubMed: 38270977
DOI: 10.1021/acsabm.3c00872 -
Analytical Chemistry Aug 2023As recently emerging nanomaterials, boron nanosheets (BNSs) have attracted more and more attention in various fields such as supercapacitors, photodetectors, bioimaging,...
As recently emerging nanomaterials, boron nanosheets (BNSs) have attracted more and more attention in various fields such as supercapacitors, photodetectors, bioimaging, and electrocatalysis due to their advantages of good biological compatibility, environmental friendliness, and good electro-optical properties. However, the study and application of BNSs in chemical and biological sensing are still in the infant stage, mainly due to the requirement of complicated, high-cost, and time-consuming preparation strategies. In this work, a new class of BNSs, namely oxidized-BNSs (i.e., ox-BNSs), were easily and rapidly synthesized by chemically treating boron powder with diluted HNO in a very short time (less than 15 min). The composition, morphology, optical property, and peroxidase mimetic activity of obtained ox-BNSs were investigated in detail. The prepared ox-BNSs were several-layered nanosheets with abundant oxygen-containing groups, emitted blue fluorescence, and possessed good intrinsic peroxidase mimetic activity, based on which a sensitive and selective colorimetric sensor was developed for detection of HO and glucose. The new easy preparation strategy and good sensing performances of the prepared ox-BNSs would greatly stimulate the study and application of BNSs in chemo- and biosensing.
Topics: Humans; Boron; Hydrogen Peroxide; Glucose; Nanostructures; Peroxidases; Colorimetry; Peroxidase; Biosensing Techniques
PubMed: 37471238
DOI: 10.1021/acs.analchem.3c01979 -
Chemosphere Jun 2022The present study discusses the ammonia (NH) sensing characteristics, photocatalytic degradation of emerging pollutants, and peroxidase mimic activity of multifunctional...
The present study discusses the ammonia (NH) sensing characteristics, photocatalytic degradation of emerging pollutants, and peroxidase mimic activity of multifunctional multi-walled carbon nanotube-tungsten oxide nanocomposite (MWCNT/WO) prepared by conventional solvothermal method. The prepared MWCNT/WO nanocomposites were characterized by various analytical techniques like XRD, Raman, XPS, N adsorption, FESEM with elemental analysis and diffuse reflection spectroscopy. The prepared 1% MWCNT/WO nanocomposite showed better gas sensing performance for the NH vapors at 10-100 ppm than the pristine WO and the response and recover time of about 13 and 15s towards 20 ppm of ammonia (NH) was achieved. The photocatalytic activity of MWCNT/WO towards organic dyes such as Rhodamine-B (Rh.B) methylene blue (MB) and pharmaceutical compound ciprofloxacin (CIP) were studied and achieved above 90% degradation at 160 min for CIP and 60 min for MB and Rho-B respectively. The radicle scavenging activity for MWCNT/WO nanocomposite showed the predominant formation of hydroxyl (OH) and superoxide radicle (O). Further, the MWCNT/WO nanocomposite showed peroxidase mimic activity and exhibit the limit of detection (LOD) of about 321 nM. From the overall analysis, MWCNT/WO hybrid seems to have potential characteristics that can be explored for multiple functional applications.
Topics: Ammonia; Ciprofloxacin; Coloring Agents; Methylene Blue; Peroxidase; Peroxidases; Photolysis
PubMed: 35227750
DOI: 10.1016/j.chemosphere.2022.134023 -
Nanoscale Aug 2023Nanozymes are increasingly being used for agricultural applications, but their adoption is limited as they are generally considered toxic, have low cost-effectiveness,...
Nanozymes are increasingly being used for agricultural applications, but their adoption is limited as they are generally considered toxic, have low cost-effectiveness, and pose complexity of fabrication. In this study, an organic compound-based, peroxidase-like nanozyme (OC nanozyme) was developed for use in the agricultural environment. This nanozyme was synthesized through a self-assembled one-pot particle synthesis process, interacting with urea and the metal ion to form a homogenous nanoparticle containing partially mimicked cofactors (Fe-N) of the natural enzyme. The OC nanozyme exhibited decent kinetic properties (HO/:0.056 mM and :2.19 μM s) and pH stability. The OC nanozyme was successfully used to detect glyphosate integrated colorimetric assay, with a good limit of detection (LOD) of at least 0.001 ng mL. The authors envision that this agricultural-friendly OC nanozyme holds great potential for a wide range of agricultural applications.
Topics: Hydrogen Peroxide; Peroxidase; Peroxidases; Colorimetry
PubMed: 37503839
DOI: 10.1039/d3nr02025h -
Food Chemistry Jun 2022Aflatoxin B (AFB), a naturally produced toxin existing in major food crops, is highly toxic and carcinogenic to human and animals. In this study, a reusable material,...
Aflatoxin B (AFB), a naturally produced toxin existing in major food crops, is highly toxic and carcinogenic to human and animals. In this study, a reusable material, Pd@PCN-222 with great adsorption performance and peroxidase-like activity was synthesized for the removal of AFB. Pd@PCN-222 exhibited great adsorption performance owing to hierarchical porous structure. Pd@PCN-222 also could catalyze the AFB in the presence of HO due to the Fe-tetrakis (4-carboxyphenyl) porphyrin and Pd as effective peroxidase active site, which improved the removal efficiency of AFB. Pd@PCN-222 was applied for the removal of AFB with a removal rate of 96.52% in 2 h. Owing to the advantages of high removal efficiency and reusability, Pd@PCN-222 had great application potential in AFB removal.
Topics: Aflatoxin B1; Animals; Humans; Hydrogen Peroxide; Metal-Organic Frameworks; Peroxidase; Peroxidases
PubMed: 35045371
DOI: 10.1016/j.foodchem.2021.132037 -
International Journal of Molecular... Jul 2023Oxidases and peroxidases have found application in the field of chlorine-free organic dye degradation in the paper, toothpaste, and detergent industries. Nevertheless,...
Oxidases and peroxidases have found application in the field of chlorine-free organic dye degradation in the paper, toothpaste, and detergent industries. Nevertheless, their widespread use is somehow hindered because of their cost, availability, and batch-to-batch reproducibility. Here, we report the catalytic proficiency of a miniaturized synthetic peroxidase, Fe-Mimochrome VI*a, in the decolorization of four organic dyes, as representatives of either the heterocyclic or triarylmethane class of dyes. Fe-Mimochrome VI*a performed over 130 turnovers in less than five minutes in an aqueous buffer at a neutral pH under mild conditions.
Topics: Peroxidase; Coloring Agents; Reproducibility of Results; Peroxidases; Catalysis
PubMed: 37446248
DOI: 10.3390/ijms241311070 -
International Journal of Biological... Apr 2024Peroxidases (EC 1.11.1.7) are involved in a wide range of physiological processes, hence their broad distribution across biological systems. These proteins can be... (Review)
Review
Peroxidases (EC 1.11.1.7) are involved in a wide range of physiological processes, hence their broad distribution across biological systems. These proteins can be classified as haem or non-haem enzymes. According to the RedOxiBase database, haem peroxidases are approximately 84 % of all known peroxidase enzymes. Class III plant peroxidases are haem-enzymes that share similar three-dimensional structures and a common catalytic mechanism for hydrogen peroxide degradation. They exist as large multigene families and are involved in metabolizing Reactive Oxygen Species (ROS), hormone synthesis and decomposition, fruit growth, defense, and cell wall synthesis and maintenance. As a result, plant peroxidases gained attention in research and became one of the most extensively studied groups of enzymes. This review provides an update on the database, classification, phylogeny, mechanism of action, structure, and physiological functions of class III plant peroxidases.
Topics: Peroxidases; Peroxidase; Plants; Reactive Oxygen Species; Heme
PubMed: 38387641
DOI: 10.1016/j.ijbiomac.2024.130306 -
Applied Microbiology and Biotechnology Jan 2023Lignocellulosic biomass is rich in lignins, which represent a bottomless natural source of aromatic compounds. Due to the high chemical complexity of these aromatic...
Lignocellulosic biomass is rich in lignins, which represent a bottomless natural source of aromatic compounds. Due to the high chemical complexity of these aromatic polymers, their biological fractionation remains challenging for biorefinery. The production of aromatics from the biological valorization of lignins requires the action of ligninolytic peroxidases and laccases produced by fungi and bacteria. Therefore, identification of efficient ligninolytic enzymes with high stability represents a promising route for lignins biorefining. Our strategy consists in exploiting the enzymatic potential of the thermophilic bacterium Thermobacillus xylanilyticus to produce robust and thermostable ligninolytic enzymes. In this context, a gene encoding a putative catalase-peroxidase was identified from the bacterial genome. The present work describes the production of the recombinant protein, its biochemical characterization, and ligninolytic potential. Our results show that the catalase-peroxidase from T. xylanilyticus is thermostable and exhibits catalase-peroxidase and manganese peroxidase activities. The electrochemical characterization using intermittent pulse amperometry showed the ability of the enzyme to oxidize small aromatic compounds derived from lignins. This promising methodology allows the fast screening of the catalase-peroxidase activity towards small phenolic molecules, suggesting its potential role in lignin transformation. KEY POINTS: • Production and characterization of a new thermostable bacterial catalase-peroxidase • The enzyme is able to oxidize many phenolic monomers derived from lignins • Intermittent pulse amperometry is promising to screen ligninolytic enzyme.
Topics: Lignin; Catalase; Peroxidase; Peroxidases; Phenols
PubMed: 36418542
DOI: 10.1007/s00253-022-12263-9