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

Santos, Carlos Henrique Corrêa dos; Talpo, Tassiana Cristina; Motta, Bruno Pereira; Kaga, Anderson Kiyoshi; Baviera, Amanda Martins; Castro, Rosane Nora; Silva, Virgínia Cláudia da; Sousa-Junior, Paulo Teixeira de; Wessjohann, Ludger A.; Carvalho, Mário Geraldo de

doi:10.1016/j.fitote.2018.12.023

Cited by 10 publications

(3 citation statements)

References 37 publications

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“…The in vitro model system of protein glycation was applied according to dos Santos et al 11 and Motta et al 12 Bovine serum albumin (BSA, 10 mg/mL; ≥96%, A6003, Sigma-Aldrich, USA) was incubated with 0.5 M glucose (≥97%, G5250, Sigma-Aldrich, USA) in 0.1 M phosphate buffer (pH 7.4) containing 0.02% sodium azide, at 37°C for 30 days. Moreover, BSA (without glucose) and BSA + glucose were incubated in the absence or presence of aminoguanidine (1 mM, prototype therapeutic agent with anti-AGE activity; 97%, 109266, Sigma-Aldrich, USA) or metformin (1 mM; 99.56% purity, Gemini Indústria de Insumos Farmacêuticos Ltda, Brazil), and in the absence or presence of quercetin (100 µM, 50 µM, 12.5 µM; ≥ 95%, Q4951, Sigma-Aldrich, USA) or rutin (100 µM, 50 µM, 12.5 µM; ≥ 94%, R5143, Sigma-Aldrich, USA).…”

Section: In Vitro Model System Of Protein Glycationmentioning

confidence: 99%

“…Protein crosslinking was assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), as described by Santos et al 11 and Motta et al 12 Reducing buffer (62.5 mM Tris-HCl, 10% glycerol, 2% SDS, 33.2 mM dithiothreitol, 0.01% bromophenol blue; pH 6.8) was added to the incubation samples. Samples containing 5 μg of protein were subjected to SDS-PAGE in 10% polyacrylamide gels.…”

Section: Protein Crosslink Formationmentioning

confidence: 99%

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Rutin inhibits the in vitroformation of advanced glycation products and protein oxidation more efficiently than quercetin

Dias

Palermo

Motta

et al. 2021

Rev. Ciênc. Farm. Básica Apl.

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Introduction:The exacerbated generation of advanced glycation end products (AGEs) triggers the onset of diabetic complications associated with hyperglycemia. The search for natural bioactive compounds that can inhibit AGE formation has gained immense interest. Quercetin and its glycoside derivative, rutin, are powerful antioxidants. They have been studied due to their potential to mitigate the disturbances observed in diabetes; however, studies comparing their antiglycation effects are limited. The aim of the present study was to compare the in vitro antiglycation potentials of quercetin and rutin. Methods: The in vitro model system of protein glycation was applied using bovine serum albumin (10 mg/mL) incubated with glucose (0.5 M) in the absence or presence of aminoguanidine (1 mM, prototype anti-AGE agent), metformin (1 mM), quercetin (100, 50, or 12.5 µM), or rutin (100, 50, or 12.5 µM). Before initiating incubations (day 0) and after 10, 20, and 30 days, aliquots were assayed for fluorescent AGEs. Markers of amino acid oxidation (dityrosine, N'-formylkynurenine, kynurenine), protein carbonyl groups (PCO), and protein crosslink formation were assessed after 30 days. Results: Both quercetin and rutin inhibited the formation of AGEs and decreased the PCO levels in a concentration-dependent manner, and moreover, the effect of rutin was more prominent than that of quercetin. Quercetin and rutin also decreased the formation of amino acid oxidation products and protein crosslinks; the best effects were observed in incubations with rutin. Conclusion: Rutin exhibited the most potent antiglycation and antioxidant activities, which may be attributed to the minor occurrence of interactions between albumin and rutin, making rutinnoside more available to exert its effects.

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Section: In Vitro Model System Of Protein Glycationmentioning

confidence: 99%

Section: Protein Crosslink Formationmentioning

confidence: 99%

Rutin inhibits the in vitroformation of advanced glycation products and protein oxidation more efficiently than quercetin

Dias

Palermo

Motta

et al. 2021

Rev. Ciênc. Farm. Básica Apl.

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“…Compound 1 , also known as sakuranetin, was first isolated from the Japanese cherry tree Puneus pseudo-cerrasus ( Asahina, 1908 ) in the early 20 th century, while compound 2 was first identified as a constituent of South-American Tessaria dodoniefolia in 1973 ( Kavka et al., 1973 ). Most recently, 1 and 2 have been reported as constituents of Siolnatria brasilensis ( dos Santos et al., 2019 ), Rhus retinorrhoea ( Mossa et al., 1996 ) and Arteminia halodendron ( Sun et al., 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Biological Properties and Absolute Configuration of Flavanones From Calceolariathyrsiflora Graham

et al. 2020

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Flavanones (-)-(2S)-5,4'-dihydroxy-7-methoxyflavanone (1) and (-)-(2S)-5,3',4'trihydroxy-7-methoxyflavanone (2) were isolated from the extracts of Calceolaria thyrsiflora Graham, an endemic perennial small shrub growing in the central zone of Chile. The absolute configuration of these compounds was resolved by optical rotation experiments and in silico calculations. Three analogs (3, 4, and 5) were synthesized to do structure-activity relationships with the biological assays studied. Biological tests revealed that only flavanone 2 exhibited a moderate inhibitory activity against the methicillinresistant strain S. aureus MRSA 97-77 (MIC value of 50 µg/ml). In addition, flavanone 2 showed a potent, selective, and competitive inhibition of 5-hLOX, which supports the traditional use of this plant as an anti-inflammatory in diseases of the respiratory tract. Also, 2 exhibited cytotoxic and selective effects against B16-F10 (8.07 ± 1.61 µM) but 4.6and 17-fold lesser activity than etoposide and taxol.

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Phytochemicals against anti‐diabetic complications: targeting the advanced glycation end product signaling pathway

et al. 2021

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

Cited by 10 publications

References 37 publications

Rutin inhibits the in vitroformation of advanced glycation products and protein oxidation more efficiently than quercetin

Rutin inhibits the in vitroformation of advanced glycation products and protein oxidation more efficiently than quercetin

Biological Properties and Absolute Configuration of Flavanones From Calceolariathyrsiflora Graham

Phytochemicals against anti‐diabetic complications: targeting the advanced glycation end product signaling pathway

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