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1.
Biomolecules ; 13(7)2023 07 21.
Artigo em Inglês | MEDLINE | ID: mdl-37509193

RESUMO

Flavonoids are a diverse group of plant-derived compounds that have been shown to have various health benefits, including anti-inflammatory effects. However, their use in the treatment of inflammatory diseases has been limited due to their low bioavailability. The nanoparticle-mediated delivery of flavonoids has been proposed as a potential solution to this issue, as it allows the sustained release of the flavonoids over time. There are several different nanoparticle systems that have been developed for flavonoid delivery, including polymeric nanoparticles, liposomes, and inorganic nanoparticles. This systematic review aims to evaluate the impact of nanoparticle-mediated delivery of flavonoids on pro-inflammatory cytokine production in various diseases. We analyzed the performance of flavonoid-encapsulated nanoparticles in regulating cytokine production in different in vitro and in vivo studies. To this end, we followed the guidelines of the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) to conduct a comprehensive search of the literature and to assess the quality of the included studies. The results showed that flavonoid-encapsulated nanoparticles significantly downregulated pro-inflammatory cytokines, such as TNF-α, IL-1ß, IL-6, and IL-18. In some cases, this effect was significantly greater than that observed with non-encapsulated flavonoids These findings suggest that nanoparticle-mediated delivery of flavonoids may have potential as a therapeutic approach for the treatment of inflammatory diseases.


Assuntos
Flavonoides , Nanopartículas , Flavonoides/farmacologia , Citocinas , Fator de Necrose Tumoral alfa , Lipossomos
2.
J Food Sci Technol ; 58(5): 1958-1968, 2021 May.
Artigo em Inglês | MEDLINE | ID: mdl-33897032

RESUMO

'Kerman' pistachios (KP; Pistacia vera L.) are an important crop for several countries but their commercial value is diminished by their shell dehiscence status and prolonged storage in popular marketplaces. The aim was to evaluate the independent/synergistic effect of prolonged storage (1-4 year) and dehiscence status (split/unsplit) on KP's morphometry and chemical composition. Whole nut's and kernel's length, width, thickness, surface area, and volume were more affected by dehiscence (split > unsplit; p ≤ 0.01) than storage time; Kernel's mass, macronutrient composition and tocopherols (T)/tocotrienols (T3) were not much affected by dehiscence but time-trend correlations were observed with macronutrient composition (split/unsplit; ρ = - 0.57-0.42) and T + T3 (unsplit; ρ = 0.81). Specific/total fatty acids were affected by a complex dehiscence × storage time interaction, and they linearly correlated with certain morphometric characteristics (r ≥ 0.6). Shell dehiscence status more than prolonged storage substantially modifies KP's quality.

3.
Molecules ; 21(12)2016 Nov 26.
Artigo em Inglês | MEDLINE | ID: mdl-27898047

RESUMO

Urease is a nickel-dependent amidohydrolase that catalyses the decomposition of urea into carbamate and ammonia, a reaction that constitutes an important source of nitrogen for bacteria, fungi and plants. It is recognized as a potential antimicrobial target with an impact on medicine, agriculture, and the environment. The list of possible urease inhibitors is continuously increasing, with a special interest in those that interact with and block the flexible active site flap. We show that disulfiram inhibits urease in Citrullus vulgaris (CVU), following a non-competitive mechanism, and may be one of this kind of inhibitors. Disulfiram is a well-known thiol reagent that has been approved by the FDA for treatment of chronic alcoholism. We also found that other thiol reactive compounds (l-captopril and Bithionol) and quercetin inhibits CVU. These inhibitors protect the enzyme against its full inactivation by the thiol-specific reagent Aldrithiol (2,2'-dipyridyl disulphide, DPS), suggesting that the three drugs bind to the same subsite. Enzyme kinetics, competing inhibition experiments, auto-fluorescence binding experiments, and docking suggest that the disulfiram reactive site is Cys592, which has been proposed as a "hinge" located in the flexible active site flap. This study presents the basis for the use of disulfiram as one potential inhibitor to control urease activity.


Assuntos
Dissulfiram/farmacologia , Inibidores Enzimáticos/farmacologia , Reagentes de Sulfidrila/farmacologia , Urease/antagonistas & inibidores , Aprovação de Drogas/legislação & jurisprudência , Cinética , Estados Unidos , United States Food and Drug Administration
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