Formation Of Fluorescent Advanced Glycation End-products Research Articles

Formation of advanced glycation end-products in silver carp (Hypophthalmichthys molitrix) surimi products during heat treatment as affected by freezing-thawing cycles

Lipid oxidation and protein degradation, along with the formation of advanced glycation end-products (AGEs), including Nε-carboxymethyl-lysine (CML), Nε-carboxyethyl-lysine (CEL) and fluorescent AGEs, in raw and subsequently heated surimi products were investigated during freezing-thawing cycles. Lipid oxidation, protein degradation, Schiff base, and AGEs formation constantly increased during freezing-thawing cycles and heat treatment (P < 0.05). Heat-induced increase of AGEs in surimi products was accelerated by freezing-thawing treatment. Formation of CML in one-stage heated (45 °C, 30 min) samples increased from 0.10 ± 0.04 to 0.53 ± 0.11 mg/kg and CEL increased from 0.03 ± 0.32 to 0.92 ± 0.74 mg/kg. In two-stage heated samples (45 °C, 30 min and 90 °C, 20 min), CML increased from 0.86 ± 0.06 to 1.12 ± 0.11 mg/kg and CEL from 1.00 ± 0.34 to 2.11 ± 1.86 mg/kg, during up to 6 freezing-thawing cycles. Formation of fluorescent AGEs derived from heating was also significantly accelerated by freezing-thawing treatment (P < 0.01). Correlation analysis suggested that the chemical synthesis of AGEs in surimi products was promoted by lipid oxidation and protein degradation during freezing-thawing cycles. AGEs formation through Schiff base oxidation likely occurred only under thermal treatment since no relationship was found between Schiff base and AGEs levels in raw surimi products.

Lactobacillus fermentum as a new inhibitor to control advanced glycation end-product formation during vinegar fermentation

The inhibitory activity of lactic acid bacteria (LAB) toward advanced glycation end-products (AGEs) during vinegar fermentation was studied, and its relationships with the substrate consumption, antioxidant capacity, total phenolic content, total flavonoid compounds, α-glucosidase, and α-amylase activity inhibition were evaluated. The vinegar was made from rice powder flour by liquid-state fermentation (LSF). The selected LAB strains were separately co-cultivated with Saccharomyces cerevisiae and Acetobacter pasteurianus 1.41 in alcoholic and acetic acid fermentation, respectively. Among 3 strains, Lactobacillus fermentum showed the strongest inhibitory effect on the formation of total fluorescent AGEs and carboxymethyl lysine (CML)/carboxyethyl lysine (CEL) in the fermentation process. The corresponding mechanisms included the acceleration of substrate consumption, improvement of antioxidant activities, and inhibition of α-glucosidase and α-amylase. In addition, the fluorescent AGEs and the CML/CEL were negatively correlated with the antioxidant activities, while the α-glucosidase and α-amylase activities were positively correlated with the total phenols and total flavonoids. Moreover, the variety of main flavor compounds increased, including esters, alcohols, phenols and acids. The results of the study support the potential use of screened LAB strains to inhibit the formation of fluorescent AGEs, CML and CEL on fermented products and in the food processing industry, without associated risks to consumers.

Ginsenoside derivatives inhibit advanced glycation end-product formation and glucose–fructose mediated protein glycation in vitro via a specific structure–activity relationship

Ginseng (Panax ginseng and red ginseng) extract has been reported to inhibit the formation of advanced glycation end-products (AGEs); however, the potential inhibitory activity of its major constituents (ginsenosides) against AGE formation is still unknown. In the present study, we investigated the inhibitory effect of ginsenoside derivatives on AGE formation. Herein, we assessed the activity of 22 ginsenosides, most of which significantly inhibited fluorescent AGE formation. Notably, ginsenoside Rh2, ginsenoside Rh1, and compound K exhibited the most potent AGE inhibitory potential with IC50 values of 3.38, 8.42, and 10.85 µM, respectively. The structure– activity relationship revealed that the presence of sugar moieties, hydroxyl groups, and their linkages, and the stereostructure of the ginsenoside skeleton played an important role in the inhibition of AGE formation. Furthermore, the inhibitory activity of the most active ginsenoside Rh2 on fructose-glucose-mediated protein glycation and oxidation of bovine serum albumin (BSA) was explored. Rh2 (0.1–12.5 µM) inhibited the formation of fluorescent AGE and non-fluorescent AGE, as well as the level of fructosamine and prevented protein oxidation by decreasing protein carbonyl formation and protein thiol group modification. Rh2 also suppressed the formation of the β-cross amyloid structure of BSA. Ginsenosides might be promising new anti-glycation agents for the prevention of diabetic complications via inhibition of AGE formation and oxidation-dependent protein damage.

New compounds of Siolmatra brasiliensis and inhibition of in vitro protein glycation damage

Twenty compounds were isolated from the hydroethanolic extract of the stems of Siolmatra brasiliensis, five flavonoids, two lignans, one glucosyl phytosterol, seven nor-cucurbitacins, one new phenolic derivative named siolmatrin (1) and four new dammarane-type saponins named siolmatrosides II-V (2–5), the structures of the compounds were assigned by means of 1D and 2D NMR experiments and HRESIMS of the natural compounds and some acetyl derivatives. The effects of the crude hydroethanolic extract (SbExt) and the ethyl acetate fraction (SbEtAc) of Siolmatra brasiliensis stems on the formation of advanced glycation end-products (AGEs) were also investigated. In the in vitro model system of protein glycation using bovine serum albumin (BSA) and glucose, addition of SbExt or SbEtAc inhibited the formation of fluorescent AGEs, in parallel to minor levels of fructosamine (SbEtAc) and markers of tyrosine and tryptophan oxidation (SbExt and SbEtAc). Protein crosslinking, which represents changes of late stages of protein glycation, was reduced in the presence of SbExt and SbEtAc. Siolmatra brasiliensis stems seem to be a promising source of compounds having ability to prevent glycoxidation changes, arising as an interesting option to be studied as a complementary therapy for complications of diabetes.

Effect of maize bran feruloylated oligosaccharides on the formation of endogenous contaminants and the appearance and textural properties of biscuits

Feruloylated oligosaccharides (FOs) have been approved by the US Food and Drug Administration for addition to baked goods. This work investigated the effect of FOs on the formation of endogenous contaminants, antioxidant properties, appearance and texture of biscuits. FOs inhibited the formation of fluorescent AGEs (advanced glycation end-products), protein oxidation products, and dicarbonyl compounds in a dose-dependent manner. Addition of 10 mg/g FOs decreased the levels of fluorescent AGEs, dityrosine, kynurenine, N′-formylkynurenine, 3-deoxyglucosone, glyoxal, and methylglyoxal by 80%, 97%, 56%, 86%, 46%, 54% and 62%, respectively. FOs might inhibit the formation of α-dicarbonyl compounds, protein oxidative products and fluorescent AGEs by enhancing antioxidant capacity and releasing ferulic acid in baked biscuits. However, FOs increased the browning and hardness of biscuits in a dose-dependent manner. Therefore, the fortification of FOs should be carefully considered based on both the expected health promoting properties and the organoleptic profile of biscuit products.

Evaluation of an olive leaf extract as a natural source of antiglycative compounds

Advanced Glycation End-products (AGEs) have been associated to diabetes, neurodegenerative and cardiovascular diseases. Mitigating the formation of AGEs is a strategy to avoid detrimental physiopathological effects of age-related chronic diseases. An olive leaf extract (OLE), obtained under acidic conditions, and two fractions, obtained by solid-phase extraction, were characterized by LC–MS/MS. Antiglycative capacity of OLE and fractions were investigated in different in vitro models. The OLE significantly inhibited the formation of Amadori products at the early stage as well as the formation of fluorescent AGEs at the advanced stage of the glycation. Carboxymethyllysine was significantly inhibited by the OLE but it showed weaker activity against argpyrimidine and carboxyethyllysine. The antiglycative activity of each OLE fraction independently did not explain the activity reached in the whole extract, being necessary the compounds present in both fractions. OLE and its fractions were highly effective for trapping reactive dicarbonyl compounds (glyoxal, methylglyoxal, 3-deoxyglucosone and 3-deoxygalactosone). Different adducts resulting from the conjugation of methylglyoxal and hydroxytyrosol in OLE were identified. Results pointed out that OLE exert a broad-spectrum in vitro antiglycative activity.

Cyanidin-3-rutinoside attenuates methylglyoxal-induced protein glycation and DNA damage via carbonyl trapping ability and scavenging reactive oxygen species.

BackgroundAdvanced glycation end-products (AGEs) play a significant role in the development and progression of vascular complication in diabetes. Anthocyanin has been recently reported to possess antiglycating activity. This study aimed to determine whether a naturally occurring anthocyanin, cyanidin-3-rutinoside (C3R) inhibits methylglyoxal (MG) induced protein glycation and oxidative protein and DNA damage.MethodsC3R (0.125–1 mM) was incubated with bovine serum albumin and MG (1 mM) for 2 weeks. The formation of fluorescent AGEs was measured by using spectrofluorometer and thiol group content were used to detect protein oxidative damage. Gel electrophoresis was used to determine whether C3R (0.125–1 mM) reduced DNA strand breakage in a glycation model comprising lysine, MG and/or Cu2+. The generation of superoxide anions and hydroxyl radicals were detected by the cytochrome c reduction assay and the thiobarbituric acid reactive substances assay. MG-trapping capacity was assessed by high performance liquid chromatography (HPLC).ResultsC3R (0.25–1 mM) reduced the formation of fluorescent AGEs and depleted protein thiol groups in bovine serum albumin mediated by MG. At 1 mM C3R inhibited oxidative DNA damage in the glycation model (p < 0.05) and at 0.5–1 mM prevented Cu2+ induced DNA strand breakage in the presence of lysine and MG. The findings showed that C3R reduced the formation of superoxide anion and hydroxyl radicals during the glycation reaction of MG with lysine. C3R directly trapped MG in a concentration and time dependent manner (both p < 0.001).ConclusionsThese findings suggest that C3R protects against MG-induced protein glycation and oxidative damage to protein and DNA by scavenging free radicals and trapping MG.

Comparison of anti-glycation capacities of several herbal infusions with that of green tea

Advanced glycation end-products (AGEs) are implicated in the pathogenesis of diabetic microvascular complications and microvascular complications of the aged. Dietary compounds that can reduce glycation may reasonably serve as valuable adjuvants, promoting the health of the aged and diabetics. This work evaluates and compares the anti-glycation activities of different herbal infusions with that of green tea, a well-documented anti-glycation beverage. The anti-glycation activity of herbal infusions were determined based on the ability of an infusion to attenuate the formation of fluorescent AGEs in glucose- and methylglyoxal-mediated protein glycation systems. All of the tested herbs except for lemongrass and rosemary—balm, mint, black tea, sage and common verbena—had potent anti-glycation abilities that exceeded or equalled that of green tea. Additionally, the amounts of phenolics and flavonoid in the herbal infusions were highly correlated with their anti-glycation activity, revealing that the anti-glycation activity of herbal infusions was primarily attributable to phenolics, particularly flavonoids.

Alginate as an antiglycating agent for human serum albumin

Hyperglycemia and the accumulation of advanced glycation endproducts (AGEs) in tissues and serum have important roles in diabetic complications. Therefore, the identification of anti-glycation compounds is attracting considerable interest. In this study, the interaction of human serum albumin (HSA) with fructose, in the absence and presence of alginate, was studied by circular dichroism, absorbance and fluorescence techniques. The characterization study of AGEs was performed using autofluorescence, fibrillar formation, the increase in absorbance and the quantification of free lysine side chains. The results indicate that alginate inhibits the fructation of HSA as observed by a reduction in the formation of fluorescent AGEs and fibrils. Furthermore, alginate reduces the amount of modified lysine side chains, signified by the lack of increase in absorbance, and increases the helicity of this protein.