Effects of Polyphenols and Their Binding With Iron
Introduction
Due to its capacity to assist in free radical formation and amplification of carcinogenic pathways. While iron is necessary for iron absorption, too much free iron can lead to various health problems, including cancer and cardiovascular disease. However, a variety of dietary components, including polyphenol compounds, have the ability to bind and have antioxidant capabilities. Some polyphenols contained in fruits and vegetables can prevent chronic diseases by binding iron and inhibiting iron-mediated processes.
Polyphenol molecules are also labile and unstable when it comes to microbial metabolism in the gastrointestinal tract. To ensure bioactivity and avoid interfering with the absorption of little bowel iron, any chemical having iron-chelating capabilities should be taken as a supplement and targeted specifically to the colon. This research aims to look into the four different types of polyphenols that can be present in a human diet. Rutin, quercetin, cyanide-3-O-glucoside, and catechin are examples of the investigated polyphenols. The iron-binding ability of these polyphenols is assessed after they are investigated for proven evidence of existence within the colon.
Isothermal Titration Microcalorimetry
The polyphenols were dissolved in potassium phosphate after rutin, quercetin, and catechin were diluted in dimethyl sulfoxide, and cyaniding 3-O-glucose was reconstituted in deionized water to provide a stock solution. FeSO4.7H20 and FeCl3.6H2O were dissolved in aqueous hydrochloric acid to make ferrous sulfate solutions and iron chloride. After that, the measurements were carried out on a VPITC MicroCalorimeter. The experiment revealed that this method is only effective under physiological settings to investigate the interaction of iron with
Furthermore, the data demonstrated that both ferric and ferrous iron bind with quercetin, and that just one iron-binding site was chosen after the estimation of the number of binding sites on quercetin. The iron-binding property of rutin was also shown to be restricted to ferrous iron, without any binding of ferric iron. Furthermore, catechin and cyanidin 3-O-glucoside revealed no significant iron-binding properties in the assay. To see if the polyphenols rutin and quercetin had an influence on intracellular levels of iron in colonocytes, RKO cells were tested with iron and cultured using and not using rutin and quercetin.
Western Bloating in Expression of Iron Metabolism Proteins
Cells exposed to quercetin and then co-cultured with iron had higher T1R1 expression than cells initially cultivated with media alone before culturing them with iron. In addition, quercetin exposed cells revealed higher T1R1expression than cells cultured with iron and afterward co-culturing them with iron. Continuous quercetin culture caused an increase in T1R1 protein expression in control cells that have not been challenged. Ferritin protein expression was the second most popular protein expression method in western blotting. Cells exposed to quercetin and subsequently co-grown with iron had reduced ferritin protein expression than cells that were media alone cultured before co-culturing them with iron. Also, pre-cultured iron cells with iron followed by continued iron culture showed a reduction in ferritin protein expression.
When compared to control cells grown in medium alone, continuous iron cultivation resulted in a considerable increase in ferritin protein expression. When polyphenols and iron were observed in the cultivated conditions at the same time, both rutin and quercetin decreased iron-related ferritin protein production, and quercetin considerably reduced intracellular iron concentrations. These findings collaborated with those on ferritin protein synthesis, implying that quercetin chelates iron extracellularly and that the iron-quercetin complex formed is not internalized. In this experiment, M stood for media alone, while Q stood for quercetin.
References
Liu, J., Wang, Y., Li, D., Wang, Y., Li, M., Chen, C… & Zhang, C. (2017). Milk protein synthesis is regulated by T1R1/T1R3, a G protein‐coupled taste receptor, through the mTOR pathway in the mouse mammary gland. Molecular Nutrition & Food Research, 61(9), 1601017. Web.
Yan, P., Xia, J. S., Chen, Y. P., Liu, Z. P., Guo, J. S., Shen, Y.,… & Wang, J. (2017). Thermodynamics of binding interactions between extracellular polymeric substances and heavy metals by isothermal titration microcalorimetry. Bioresource Technology, 232, 354-363. Web.