Synergistic effect of spermidine and ciprofloxacin against Alzheimer's disease in male rat via ferroptosis modulation.

Alzheimer's disease (AD) is a prevalent form of neurodegenerative disease with a complex pathophysiology that remains not fully understood, and the exact mechanism of neurodegeneration is uncertain. Ferroptosis has been linked to the progression of degenerative diseases observed in AD models. The present study is designed to investigate the protective effects of spermidine, a potent antioxidant and iron chelator, and its synergistic interactions with ciprofloxacin, another iron chelator, in modulating ferroptosis and mitigating AD progression in rats. This study investigated AD-related biomarkers like neurotoxic amyloid beta (Aß), arginase I, and serotonin. Spermidine demonstrated an anti-ferroptotic effect in the AD model, evident from the modulation of ferroptosis parameters such as hippocampus iron levels, reduced protein expression of transferrin receptor 1 (TFR1), and arachidonate 15-lipoxygenase (ALOX15). Additionally, the administration of spermidine led to a significant increase in protein expression of phosphorylated nuclear factor erythroid 2-related factor 2 (p-Nrf2) and upregulation of Cystine/glutamate transporter (SLC7A11) gene expression. Moreover, spermidine notably decreased p53 protein levels, acrolein, and gene expression of spermidine/spermine N1-acetyltransferase 1 (SAT1). Overall, our findings suggest that spermidine and/or ciprofloxacin may offer potential benefits against AD by modulating ferroptosis. Furthermore, spermidine enhanced the antioxidant efficacy of ciprofloxacin and reduced its toxic effects.

Withdrawal Notice: Role of Zinc Oxide Nanoparticles Synthesized by Fenugreek Seeds Extract as Anticancer Agent: In Vitro and In Vivo Studies

The article has been withdrawn on the recommendation of the Editor-in-Chief of the journal Anti-Cancer Agents in Medicinal Chemistry due to some inconsistencies in the content of the article. Bentham Science apologizes to the readers of the journal for any inconvenience this may have caused. The Bentham Editorial Policy on Article Withdrawal can be found at https://benthamscience.com/editorial-policiesmain.php Bentham Science Disclaimer: It is a condition of publication that manuscripts submitted to this journal have not been published and will not be simultaneously submitted or published elsewhere. Furthermore, any data, illustration, structure or table that has been published elsewhere must be reported, and copyright permission for reproduction must be obtained. Plagiarism is strictly forbidden, and by submitting the article for publication the authors agree that the publishers have the legal right to take appropriate action against the authors, if plagiarism or fabricated information is discovered. By submitting a manuscript, the authors agree that the copyright of their article is transferred to the publishers if and when the article is accepted for publication.

Alzheimer's disease improved through the activity of mitochondrial chain complexes and their gene expression in rats by boswellic acid.

The foremost neurodegenerative disease is Alzheimer's (AD), which is characterized as a gradual decrease in memory, cognitive function, and also personal changes occurred. This study aims to assess the role of boswellic bioactive component in control Alzheimer's disease through enhancing mitochondrial electron transport chain complexes in the rat model. Rats were divided into five equal groups: the control group (G1), boswellic acid control group (G2), AD disease group (G3), boswellic acid -pre-treated group (G4) and boswellic acid-treated group (G5). At the end of the experiment, blood glucose level, tau protein, different neurochemicals parameters (dopamine, acetylcholine), L-malondialdehyde (MDA) levels, and superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx) activities was determined. Also, GLUT2 and mitochondrial electron transport chain complexes were evaluated. As a result, an increase in hippocampus glucose, tau protein expression, MDA and GLUT2 in the AD group (G3) compared to control groups (G1 and G2) has been recorded. These parameters were declined after pre (G4) and treated (G5) by boswellic acid. The neurochemicals, antioxidants parameters, four mitochondrial chain complexes activities and their gene expression in the hippocampus of the AD group were decreased compared to the control groups (G1 and G2). In contrast, pre and treated groups by boswellic acid (G4 and G5, respectively) have shown an increase in antioxidants parameters, and the activities of four mitochondrial complexes, with the best improvement in the pre-treated group (G4), then treated group (G5). In conclusion; the boswellic acid improved the antioxidant and mitochondrial complexes in Alzheimer's disease.

Immobilization of horseradish peroxidase into cubic mesoporous silicate, SBA-16 with high activity and enhanced stability.

Mesoporous silicate, SBA-16 is one of the most promising supports for horseradish peroxidase. In this study, SBA-16 was synthesized, and the anchored HRP enzyme in the organized porous networks, SBA-16. The mesoporous material, SBA-16 and the anchored HRP enzyme were characterized by Fourier transform infrared, scanning electron microscopy, transmission electron microscopy, N2 adsorption-desorption isotherms, low-angle XRD and thermogravimetric analysis. The percentage of immobilized HRP was 57%. The enzyme affinity constant, Km values of soluble and immobilized enzyme were 5.27 and 3.9 mM for hydrogen peroxide and 12 and 10.4 mM for guiacol, respectively, indicating that the immobilized enzyme had more affinity to the substrate than free HRP. Also, the free and immobilized enzyme had pH and temperature optima at 5.6, and 40 °C, respectively. The free enzyme was stable at 40 °C but that for the immobilized enzyme was detected up to 60 °C. Reusability of immobilized enzyme was found to be 10 cycles; the immobilized enzyme can only retain 50% of its activity after 5 cycles. The results indicate the higher efficiency, stability, and reusability of the immobilized enzyme than free enzyme. The HRP immobilized to SBA-16 due to the large surface area, and narrow pore size distribution of SBA-16.

Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics.

Ulocladium atrum inulinase was immobilized on different composite membranes composed of chitosan/nonwoven fabrics. Km values of free and immobilized U. atrum inulinase on different composite membranes were calculated. The enzyme had optimum pH at 5.6 for free and immobilized U. atrum inulinase on polyester nonwoven fabric coated with 3 percent chitosan solution (PPNWF3), but optimum pH was 5 for immobilized U. atrum inulinase on polyester and polypropylene nonwoven fabrics coated with 1 percent chitosan solution. The enzyme had optimum temperature at 40 degree C for immobilized enzyme on each of polyester and polypropylene composite membranes coated with 1 percent chitosan, while it was 50 degree C for free and immobilized enzyme on polypropylene nonwoven fabric coated with 3 percent chitosan solution. Free U. atrum inulinase was stable at 40 degree C but thermal stability of the immobilized enzyme was detected up to 60 degree C. Reusability of immobilized enzyme was from 38 to 42 cycles of reuse; after this, the immobilized enzyme lost its activity completely. In conclusion, immobilized U. atrum inulinase was considerably more stable than the free enzyme, and could be stored for extended periods.