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

AI Article Synopsis

  • Ginseng extract, specifically its ginsenoside components, has been found to inhibit the formation of advanced glycation end-products (AGEs), which are linked to various health issues.
  • A study tested 22 different ginsenosides, identifying Rh2, Rh1, and compound K as the most effective at blocking AGE formation, with Rh2 showing the strongest results.
  • Rh2 not only inhibited AGE formation but also prevented protein oxidation and alterations in important protein structures, suggesting that ginsenosides could be useful in preventing complications from diabetes.

Article Abstract

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 IC 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.

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Source
http://dx.doi.org/10.1016/j.bioorg.2021.104844DOI Listing

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