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Prunin from (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin. | LitMetric

AI Article Synopsis

  • - The study explores the connection between diabetes complications and two factors: aldose reductase (AR) and advanced glycation end products (AGEs), focusing on natural compounds to reduce their effects.
  • - Through bioassay-guided isolation, 10 flavonoids and one coumarin were isolated from a plant, showing that prunin, narirutin, and naringin effectively inhibit both human and rat AR at low concentrations.
  • - Prunin not only prevents the formation of AGEs and protein damage from oxidation but also inhibits the formation of harmful protein structures, suggesting its potential role in reducing diabetes complications.

Article Abstract

Diabetes complications are associated with aldose reductase (AR) and advanced glycation end products (AGEs). Using bioassay-guided isolation by column chromatography, 10 flavonoids and one coumarin were isolated from Rafin and tested in vitro for an inhibitory effect against human recombinant AR (HRAR) and rat lens AR (RLAR). Prunin, narirutin, and naringin inhibited RLAR (IC 0.48-2.84 μM) and HRAR (IC 0.68-4.88 μM). Docking simulations predicted negative binding energies and interactions with the RLAR and HRAR binding pocket residues. Prunin (0.1 and 12.5 μM) prevented the formation of fluorescent AGEs and nonfluorescent N-(carboxymethyl) lysine (CML), as well as the fructose-glucose-mediated protein glycation and oxidation of human serum albumin (HSA). Prunin suppressed the formation of the β-cross-amyloid structure of HSA. These results indicate that prunin inhibits oxidation-dependent protein damage, AGE formation, and AR, which may help prevent diabetes complications.

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Source
http://dx.doi.org/10.1021/acs.jafc.3c09716DOI Listing

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