Gotowe bibliografie tematyczne / Glycation inhibitors

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Artykuły w czasopismach

Gotowa bibliografia na temat „Glycation inhibitors”

Autor: Grafiati

Data publikacji: 6 września 2023

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Artykuły w czasopismach na temat "Glycation inhibitors"

Perera, HKI, and DCR Wijetunge. "A novel in vitro method to detect inhibitors of protein glycation." Asian Journal of Medical Sciences 5, no. 3 (2014): 15–21. http://dx.doi.org/10.3126/ajms.v5i3.8670.

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Background: Protein glycation generates advanced glycation end products (AGEs) which are implicated in the pathogenesis of chronic complications associated with diabetes. Identifi cation of medicinal plants with protein glycation inhibitory potential will enhance the opportunity to delay or inhibit diabetic complications with minimum side effects. Techniques available to identify protein glycation inhibitors require expensive specialized equipment. Objective: Objective of this study was to develop a relatively simple in vitro method to identify the protein glycation inhibitory potential of compounds or medicinal plants. Methods: Bovine serum albumin (BSA) was incubated with different concentrations of glucose or fructose or ribose for 31 days at pH 7.4. Standard inhibitor aminoguanidine (AG) was used as a positive control. Effect on the BSA migration under different experimental conditions was compared using polyacrylamide gel electrophoresis under native conditions (PAGE). Murraya koenigii leaf extract was analyzed for its effect on protein glycation. Results: We demonstrated many aspects of protein glycation including the effect of sugar concentration, type of the sugar and incubation period on protein glycation using this comparatively simpler method, which was previously, demonstrated using more sophisticated and expensive equipment. Migration of the BSA band towards the anode was proportionate to the degree of protein glycation. Further, we were innovative in demonstrating the inhibitory effect of AG on protein glycation using PAGE. BSA migration was comparatively slower when AG was included in the presence of sugar, indicating its inhibitory effects. We also revealed the protein glycation inhibitory potential of Murraya koenigii leaf extract, which was greater than that of AG at the concentrations used in the study. Conclusion: We have developed novel simple in vitro method using PAGE to identify inhibitors of protein glycation. Asian Journal of Medical Science, Volume-5(3) 2014: 15-21 http://dx.doi.org/10.3126/ajms.v5i3.8670

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E-FARAN, MISS GULL, MUHAMMAD ANJUM ZIA, and NIGHAT ASLAM. "EFFECT OF CAPTOPRIL." Professional Medical Journal 19, no. 01 (2012): 078–85. http://dx.doi.org/10.29309/tpmj/2012.19.01.1929.

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Objectives: (1) To investigate the inhibitory effect of Captopril on level of glycation (in vivo). (2) To study glycation inhibition invivo. Study design: Case study. Period: Sep. 2006 to March. 2008. One year seven months. Setting: Department of Biochemistry Universityof Agriculture, Faisalabad. Methods: Different parameters like fluorescence, total proteins, TBA (thiobarbituric acid) method, periodateborohydride assay were used to check the effect of inhibitor on glycation. Thirty two combinations were made and all these combinations wereplaced at 37̊C, at same time for five weeks. 3mL of blood sample was drawn after 1st, 3rd and 5th week of incubation to perform the experimentsfor glycation and glycation inhibition. Along with the same temperature (37̊C), different combinations of glucose and inhibitor were used.Results: Effective concentration of inhibitor helped to decrease the level of glycation. All concentrations of glucose (G , G and G ) showed 1 2 3glycation with protein. The inhibitor Captopril (all concentrations) showed variations in inhibition of glycation at one temperature (37̊C) withdifferent parameters (Fluorescence, TBA and Periodate) but the most effective concentration of inhibitors at each condition is I (1mM) but I (10 3 1mM) and I (5 mM) were also equally effective after I . Periodate borohydride Assay is more effective for glycation determination than 2 3thiobarbituric acid assay. Conclusions: Captopril can be used as glycation inhibitor in future. As it enhances the activity of transketolase, it canproduce 3DG compound which can block the AGEs. However, more experimentations should be done on animal or on large scale before itsapplication in diabetic patients.

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Pawlukianiec, Cezary, Małgorzata Ewa Gryciuk, Kacper Maksymilian Mil, Małgorzata Żendzian-Piotrowska, Anna Zalewska, and Mateusz Maciejczyk. "A New Insight into Meloxicam: Assessment of Antioxidant and Anti-Glycating Activity in In Vitro Studies." Pharmaceuticals 13, no. 9 (2020): 240. http://dx.doi.org/10.3390/ph13090240.

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Meloxicam is a non-steroidal anti-inflammatory drug, which has a preferential inhibitory effect to cyclooxyganase-2 (COX-2). Although the drug inhibits prostaglandin synthesis, the exact mechanism of meloxicam is still unknown. This is the first study to assess the effect of meloxicam on protein glyco-oxidation as well as antioxidant activity. For this purpose, we used an in vitro model of oxidized bovine serum albumin (BSA). Glucose, fructose, ribose, glyoxal and methylglyoxal were used as glycating agents, while chloramine T was used as an oxidant. We evaluated the antioxidant properties of albumin (2,2-di-phenyl-1-picrylhydrazyl radical scavenging capacity, total antioxidant capacity and ferric reducing antioxidant power), the intensity of protein glycation (Amadori products, advanced glycation end products) and glyco-oxidation (dityrosine, kynurenine, N-formylkynurenine, tryptophan and amyloid-β) as well as the content of protein oxidation products (advanced oxidation protein products, carbonyl groups and thiol groups). We have demonstrated that meloxicam enhances the antioxidant properties of albumin and prevents the protein oxidation and glycation under the influence of various factors such as sugars, aldehydes and oxidants. Importantly, the antioxidant and anti-glycating activity is similar to that of routinely used antioxidants such as captopril, Trolox, reduced glutathione and lipoic acid as well as protein glycation inhibitors (aminoguanidine). Pleiotropic action of meloxicam may increase the effectiveness of anti-inflammatory treatment in diseases with oxidative stress etiology.

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West, Brett J., Shixin Deng, Akemi Uwaya, et al. "Iridoids are natural glycation inhibitors." Glycoconjugate Journal 33, no. 4 (2016): 671–81. http://dx.doi.org/10.1007/s10719-016-9695-x.

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Hosseini, Asieh, and Mohammad Abdollahi. "Diabetic Neuropathy and Oxidative Stress: Therapeutic Perspectives." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/168039.

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Diabetic neuropathy (DN) is a widespread disabling disorder comprising peripheral nerves' damage. DN develops on a background of hyperglycemia and an entangled metabolic imbalance, mainly oxidative stress. The majority of related pathways like polyol, advanced glycation end products, poly-ADP-ribose polymerase, hexosamine, and protein kinase c all originated from initial oxidative stress. To date, no absolute cure for DN has been defined; although some drugs are conventionally used, much more can be found if all pathophysiological links with oxidative stress would be taken into account. In this paper, although current therapies for DN have been reviewed, we have mainly focused on the links between DN and oxidative stress and therapies on the horizon, such as inhibitors of protein kinase C, aldose reductase, and advanced glycation. With reference to oxidative stress and the related pathways, the following new drugs are under study such as taurine, acetyl-L-carnitine, alpha lipoic acid, protein kinase C inhibitor (ruboxistaurin), aldose reductase inhibitors (fidarestat, epalrestat, ranirestat), advanced glycation end product inhibitors (benfotiamine, aspirin, aminoguanidine), the hexosamine pathway inhibitor (benfotiamine), inhibitor of poly ADP-ribose polymerase (nicotinamide), and angiotensin-converting enzyme inhibitor (trandolapril). The development of modern drugs to treat DN is a real challenge and needs intensive long-term comparative trials.

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Julius, Angeline, and Waheeta Hopper. "INHIBITION OF ADVANCED GLYCATION END-PRODUCT FORMATION BY QUERCETIN AND CATECHIN: AN ALTERNATIVE THERAPY FOR TREATING DIABETIC COMPLICATIONS." Asian Journal of Pharmaceutical and Clinical Research 10, no. 11 (2017): 173. http://dx.doi.org/10.22159/ajpcr.2017.v10i11.19412.

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Objective: The objective of this research was to determine early advanced glycation end-product (AGE) inhibition by natural aldose reductase inhibitors (ARIs), quercetin and catechin.Methods: The assay mixture (4 ml) consisted of 2 ml of 50 mM phosphate-buffered saline (pH 7.4), 50 μg/μl bovine serum albumin (BSA), and 2 mM glucose with or without the inhibitor. The test samples were treated with three different concentrations (10 mM, 20 mM, and 40 mM) of quercetin and catechin. High-throughput screening-based assay was adapted to perform the BSA-glucose test to determine the induction of AGE formation and its inhibition by quercetin, and catechin, using the fluorescence of the AGE-BSA sample at excitation and emission wavelengths of 350 and 450 nm.Result: The ARIs, quercetin and catechin inhibited early glycation with an inhibitory concentration value of 15.58 mM and 35.01 mM, respectively.Conclusion: The suppression of AGEs formation by natural inhibitors of aldose reductase would provide an alternative approach to the control of diabetic complications.

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Pervez, Humayun, Nazia Khan, Jamshed Iqbal, et al. "Synthesis, crystal structure, molecular docking studies and bio-evaluation of some N4-benzyl-substituted isatin- 3-thiosemicarbazones as urease and glycation inhibitors." Heterocyclic Communications 24, no. 1 (2018): 51–58. http://dx.doi.org/10.1515/hc-2017-0148.

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Abstract Fifteen N4-benzyl-substituted isatin-3-thiosemicarbazones 5a–o were synthesized and evaluated for their urease and glycation inhibitory potential. Lemna aequinocitalis growth and Artemia salina assays were also done to determine their phytotoxic and toxic effects. All compounds are potent inhibitors of the urease enzyme, displaying inhibition [half maximal inhibitory concentration (IC50)=1.08±0.12–11.23±0.19 μm] superior to that of the reference inhibitor thiourea (IC50=22.3±1.12 μm). Compounds 5c, 5d, 5h, 5j,k are potent antiglycating agents, showing glycation inhibitory activity better than that of the reference inhibitor rutin (IC50 values 209.87±0.37–231.70±6.71 vs. 294.5±1.5 μm). In the phytotoxicity assay, 11 thiosemicarbazones 5a–d, 5g, 5h, 5j–l, 5n,o are active, demonstrating 5–100% growth inhibition of L. aequinocitalis at the highest tested concentrations (1000 or 500 μg/mL). In the brine shrimp (A. salina) lethality bioassay, three derivatives 5b, 5j and 5o are active with median lethal dose (LD50) values of 3.63×10−5, 2.90×10−5 and 2.31×10−4 m, respectively.

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Starowicz, Małgorzata, and Henryk Zieliński. "Inhibition of Advanced Glycation End-Product Formation by High Antioxidant-Leveled Spices Commonly Used in European Cuisine." Antioxidants 8, no. 4 (2019): 100. http://dx.doi.org/10.3390/antiox8040100.

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Spices and herbs, as good sources of polyphenols, could be strong inhibitors of advanced glycation end-product (AGE) formation. The aim of this research was to measure the ability of various spices to inhibit AGEs and to study the correlation of AGE inhibition with total phenolic (TP) content and antioxidant capacity. Fourteen spices commonly used in European cuisine were extracted with a 50% ethanol solution, and their water and total phenolic contents and antioxidant capacities were examined. Antioxidant capacity was evaluated using three methods: (1) Measurement of the radical scavenging ability of 2,2’-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and (2) 2,2-diphenyl-1-picrylhydrazyl (DPPH●); and (3) photochemiluminescence (PCL) assay. Antiglycation properties were studied in vivo using two model systems: Bovine serum albumin-glucose (BSA-glucose) and bovine serum albumin-methylglyoxal (BSA-MGO). The most potent glycation inhibitors, according to the BSA-MGO assay, were star anise (88%), cinnamon (85%), allspice (81%), and cloves (79%), whereas in the BSA-glucose measurement, oregano was noted to be a very effective inhibitor of the glycation process. The ability to inhibit glycation was highly correlated with TP values in the BSA-MGO and BSA-glucose assay (r = 0.84 and 0.76, respectively). Our research showed the high antiglycation ability of cinnamon, cloves, and allspice, and we suggest, for the first time, that anise could also be considered a good glycation inhibitor.

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Rahbar, Samuel, and James L. Figarola. "Novel inhibitors of advanced glycation endproducts." Archives of Biochemistry and Biophysics 419, no. 1 (2003): 63–79. http://dx.doi.org/10.1016/j.abb.2003.08.009.

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Rahbar, Samuel, Kiran Kumar Yernini, Stephen Scott, Noe Gonzales, and Iraj Lalezari. "Novel Inhibitors of Advanced Glycation Endproducts." Biochemical and Biophysical Research Communications 262, no. 3 (1999): 651–56. http://dx.doi.org/10.1006/bbrc.1999.1275.

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